PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16814740-1 2006 Cytochrome b5 reductase (cb5r), a member of the flavoprotein transhydrogenase family of oxidoreductase enzymes, catalyzes the transfer of reducing equivalents from the physiological electron donor, NADH, to two molecules of cytochrome b5. NAD 198-202 cytochrome b5 type A Homo sapiens 224-237 17489100-4 2007 To avoid the accumulation of metHb, reductive pathways mediated by cytochrome b5 or flavin, coupled with NADH-dependent or NADPH-dependent metHb reductases, respectively, keep the level of metHb in erythrocytes at less than 1% of the total hemoglobin under normal conditions. NAD 105-109 cytochrome b5 type A Homo sapiens 67-80 17489100-8 2007 In contrast, the cytochrome b5-NADH pathway becomes dominant under conditions of excess metHb accumulation, only after the capacity of the flavin-NADPH pathway has reached its limit. NAD 31-35 cytochrome b5 type A Homo sapiens 17-30 15986701-2 2004 A bacterial flavoprotein, putidaredoxin reductase (PdR), was activated and shown to be capable of catalyzing the electron transport from NADH to electron-carrier proteins such as cytochrome b5 (tCyt-b5) and putidaredoxin (Pdx) in reverse micelles. NAD 137-141 cytochrome b5 type A Homo sapiens 179-192 23045123-1 2005 NADH cytochrome b(5) reductase (b(5)R; EC 1.6.2.2; Diaphorase I; NADH: ferricytochrome b(5) oxidoreductase) is an FAD-containing protein, which, along with the hemoprotein cytochrome b(5) (cyt b(5)), mediates electron transfer from NADH to fatty acid desaturases, P450 oxidases, methemoglobin, and ascorbyl free radical. NAD 0-4 cytochrome b5 type A Homo sapiens 5-20 23045123-1 2005 NADH cytochrome b(5) reductase (b(5)R; EC 1.6.2.2; Diaphorase I; NADH: ferricytochrome b(5) oxidoreductase) is an FAD-containing protein, which, along with the hemoprotein cytochrome b(5) (cyt b(5)), mediates electron transfer from NADH to fatty acid desaturases, P450 oxidases, methemoglobin, and ascorbyl free radical. NAD 0-4 cytochrome b5 type A Homo sapiens 76-91 23045123-1 2005 NADH cytochrome b(5) reductase (b(5)R; EC 1.6.2.2; Diaphorase I; NADH: ferricytochrome b(5) oxidoreductase) is an FAD-containing protein, which, along with the hemoprotein cytochrome b(5) (cyt b(5)), mediates electron transfer from NADH to fatty acid desaturases, P450 oxidases, methemoglobin, and ascorbyl free radical. NAD 0-4 cytochrome b5 type A Homo sapiens 189-197 15047725-7 2004 The recombinant soluble cytochrome b(5) showed an asymmetrical absorption spectrum at 560 nm as is shown by mammalian cytochromes b(5) upon reduction with NADH and NADH-cytochrome b(5) reductase. NAD 155-159 cytochrome b5 type A Homo sapiens 24-39 12646278-2 2003 To determine whether electron input via the NADH-dependent pathway was similarly functional in whole cells and necessary for the stimulation by cytochrome b(5), we constructed five plasmids designed to express human CYP2E1 in various combinations with cytochrome b(5) reductase, cytochrome b(5), and cytochrome P450 reductase. NAD 44-48 cytochrome b5 type A Homo sapiens 144-158 9588172-1 1998 To identify the cytochrome b5 residues responsible for the electrostatic interaction with NADH-cytochrome b5 reductase (b5R), we prepared and characterized the cytochrome b5 mutants in which Glu41, Glu42, Glu63, Asp70, and Glu73 were replaced by Ala, utilizing site-directed mutagenesis and the expression system for cytochrome b5 in Escherichia coli. NAD 90-94 cytochrome b5 type A Homo sapiens 16-29 11695905-0 2001 The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent. NAD 34-38 cytochrome b5 type A Homo sapiens 49-62 11695905-1 2001 Cytochrome b5 reductase (cb5r) (EC 1.6.6.2) catalyzes the reduction of two molecules of cytochrome b5 using NADH as the physiological electron donor. NAD 108-112 cytochrome b5 type A Homo sapiens 0-13 11695905-1 2001 Cytochrome b5 reductase (cb5r) (EC 1.6.6.2) catalyzes the reduction of two molecules of cytochrome b5 using NADH as the physiological electron donor. NAD 108-112 cytochrome b5 type A Homo sapiens 88-101 11123803-1 2000 Plant cytochrome b5 reductases (b5R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b5) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. NAD 106-110 cytochrome b5 type A Homo sapiens 6-19 11123803-1 2000 Plant cytochrome b5 reductases (b5R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b5) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. NAD 106-110 cytochrome b5 type A Homo sapiens 136-149 11123803-1 2000 Plant cytochrome b5 reductases (b5R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b5) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. NAD 106-110 cytochrome b5 type A Homo sapiens 151-157 9588172-1 1998 To identify the cytochrome b5 residues responsible for the electrostatic interaction with NADH-cytochrome b5 reductase (b5R), we prepared and characterized the cytochrome b5 mutants in which Glu41, Glu42, Glu63, Asp70, and Glu73 were replaced by Ala, utilizing site-directed mutagenesis and the expression system for cytochrome b5 in Escherichia coli. NAD 90-94 cytochrome b5 type A Homo sapiens 95-108 9588172-1 1998 To identify the cytochrome b5 residues responsible for the electrostatic interaction with NADH-cytochrome b5 reductase (b5R), we prepared and characterized the cytochrome b5 mutants in which Glu41, Glu42, Glu63, Asp70, and Glu73 were replaced by Ala, utilizing site-directed mutagenesis and the expression system for cytochrome b5 in Escherichia coli. NAD 90-94 cytochrome b5 type A Homo sapiens 95-108 9588172-1 1998 To identify the cytochrome b5 residues responsible for the electrostatic interaction with NADH-cytochrome b5 reductase (b5R), we prepared and characterized the cytochrome b5 mutants in which Glu41, Glu42, Glu63, Asp70, and Glu73 were replaced by Ala, utilizing site-directed mutagenesis and the expression system for cytochrome b5 in Escherichia coli. NAD 90-94 cytochrome b5 type A Homo sapiens 95-108 8561495-1 1996 NADH-dependent testosterone 6 beta-hydroxylation and nifedipine oxidation activities could be reconstituted in systems containing cytochrome b5 (b5), NADH-b5 reductase, and bacterial recombinant cytochrome P450 (P450) 3A4 with a synthetic phospholipid mixture, cholate, MgCl2, and reduced glutathione. NAD 0-4 cytochrome b5 type A Homo sapiens 130-143 9586947-6 1998 NADH was as effective as NADPH in promoting microsomal AZT reduction, raising the possibility of cytochrome b5 (b5) involvement. NAD 0-4 cytochrome b5 type A Homo sapiens 97-110 8694855-1 1996 NADH-dependent 7-ethoxycoumarin O-deethylation activities could be reconstituted in systems containing cytochrome b5 (b5), NADH-b5 reductase, and bacterial recombinant P450 2E1 in 100 mM potassium phosphate buffer (pH 7.4) containing a synthetic phospholipid mixture and cholate. NAD 0-4 cytochrome b5 type A Homo sapiens 103-116 8660685-0 1996 Interaction of ferric complexes with NADH-cytochrome b5 reductase and cytochrome b5: lipid peroxidation, H2O2 generation, and ferric reduction. NAD 37-41 cytochrome b5 type A Homo sapiens 42-55 8660685-0 1996 Interaction of ferric complexes with NADH-cytochrome b5 reductase and cytochrome b5: lipid peroxidation, H2O2 generation, and ferric reduction. NAD 37-41 cytochrome b5 type A Homo sapiens 70-83 8660685-2 1996 NADH-dependent microsomal electron transfer involves the enzymes NADH-cytochrome b5 reductase and cytochrome b5. NAD 0-4 cytochrome b5 type A Homo sapiens 70-83 8660685-2 1996 NADH-dependent microsomal electron transfer involves the enzymes NADH-cytochrome b5 reductase and cytochrome b5. NAD 0-4 cytochrome b5 type A Homo sapiens 98-111 8622631-9 1996 Anti-cytochrome b5 IgG decreased NADPH- and NADH-dependent HER formation, and this was associated with inhibition of superoxide formation with both reductants. NAD 44-48 cytochrome b5 type A Homo sapiens 5-18 7733677-0 1995 Transient kinetics of intracomplex electron transfer in the human cytochrome b5 reductase-cytochrome b5 system: NAD+ modulates protein-protein binding and electron transfer. NAD 112-116 cytochrome b5 type A Homo sapiens 66-79 8554320-0 1995 Role of cytochrome b5 in NADH-dependent microsomal reduction of ferric complexes, lipid peroxidation, and hydrogen peroxide generation. NAD 25-29 cytochrome b5 type A Homo sapiens 8-21 8554320-1 1995 The NADH-dependent microsomal electron transfer system consists of NADH-cytochrome b5 reductase and cytochrome b5, which donates reducing equivalents to fatty acyl desaturase, cytochrome P450, and other reactions. NAD 4-8 cytochrome b5 type A Homo sapiens 72-85 8554320-1 1995 The NADH-dependent microsomal electron transfer system consists of NADH-cytochrome b5 reductase and cytochrome b5, which donates reducing equivalents to fatty acyl desaturase, cytochrome P450, and other reactions. NAD 4-8 cytochrome b5 type A Homo sapiens 100-113 8653076-0 1995 The reducing ability of iron chelates by NADH-cytochrome B5 reductase or cytochrome B5 responsible for NADH-supported lipid peroxidation. NAD 41-45 cytochrome b5 type A Homo sapiens 46-59 7733677-0 1995 Transient kinetics of intracomplex electron transfer in the human cytochrome b5 reductase-cytochrome b5 system: NAD+ modulates protein-protein binding and electron transfer. NAD 112-116 cytochrome b5 type A Homo sapiens 90-103 2264826-4 1990 The cytochrome b5 was reduced in the membrane preparations by NADH, demonstrating the presence of an NADH: cytochrome b5 reductase; NADPH was a less effective donor. NAD 62-66 cytochrome b5 type A Homo sapiens 4-17 8358221-3 1993 One of the fractions, which bound to a cellulose phosphate column, was able to reduce the soluble cytochrome b5, using NADH as an electron donor. NAD 119-123 cytochrome b5 type A Homo sapiens 98-111 1897935-7 1991 Pretreatment of microsomes with an antibody to cytochrome b5 reductase inhibited microsomal NADH-dependent reduction of DES Q to DES by 55%. NAD 92-96 cytochrome b5 type A Homo sapiens 47-60 1898726-0 1991 Structural role of serine 127 in the NADH-binding site of human NADH-cytochrome b5 reductase. NAD 37-41 cytochrome b5 type A Homo sapiens 69-82 1898726-9 1991 Ser-127----Pro mutant and Ser-127----Ala mutant showed very low Kcat/Km (NADH) values (5 x 10(7) and 3.5 x 10(7) s-1 M-1, respectively) with cytochrome b5 as an electron acceptor, than that of the wild-type enzyme (Kcat/Km (NADH) = 179 x 10(7) s-1 M-1), while the Kcat/Km (cytochrome b5) value for each enzyme was similar. NAD 73-77 cytochrome b5 type A Homo sapiens 141-154 1898726-9 1991 Ser-127----Pro mutant and Ser-127----Ala mutant showed very low Kcat/Km (NADH) values (5 x 10(7) and 3.5 x 10(7) s-1 M-1, respectively) with cytochrome b5 as an electron acceptor, than that of the wild-type enzyme (Kcat/Km (NADH) = 179 x 10(7) s-1 M-1), while the Kcat/Km (cytochrome b5) value for each enzyme was similar. NAD 73-77 cytochrome b5 type A Homo sapiens 273-286 8226835-0 1993 Interaction of non-myristoylated NADH-cytochrome b5 reductase with cytochrome b5-dimyristoylphosphatidylcholine vesicles. NAD 33-37 cytochrome b5 type A Homo sapiens 38-51 8226835-0 1993 Interaction of non-myristoylated NADH-cytochrome b5 reductase with cytochrome b5-dimyristoylphosphatidylcholine vesicles. NAD 33-37 cytochrome b5 type A Homo sapiens 67-80 2264826-4 1990 The cytochrome b5 was reduced in the membrane preparations by NADH, demonstrating the presence of an NADH: cytochrome b5 reductase; NADPH was a less effective donor. NAD 62-66 cytochrome b5 type A Homo sapiens 107-120 2264826-4 1990 The cytochrome b5 was reduced in the membrane preparations by NADH, demonstrating the presence of an NADH: cytochrome b5 reductase; NADPH was a less effective donor. NAD 101-105 cytochrome b5 type A Homo sapiens 4-17 2264826-4 1990 The cytochrome b5 was reduced in the membrane preparations by NADH, demonstrating the presence of an NADH: cytochrome b5 reductase; NADPH was a less effective donor. NAD 101-105 cytochrome b5 type A Homo sapiens 107-120 2264826-7 1990 The addition of oleoyl-CoA to the NADH-reduced membranes resulted in the CN(-)-sensitive partial re-oxidation of cytochrome b5, indicating that electrons from NADH were transferred to the site of desaturation via this cytochrome. NAD 34-38 cytochrome b5 type A Homo sapiens 113-126 2264826-7 1990 The addition of oleoyl-CoA to the NADH-reduced membranes resulted in the CN(-)-sensitive partial re-oxidation of cytochrome b5, indicating that electrons from NADH were transferred to the site of desaturation via this cytochrome. NAD 159-163 cytochrome b5 type A Homo sapiens 113-126 2264826-8 1990 The delta 12-desaturase in safflower, therefore, is CN(-)-sensitive and appears to require cytochrome b5 and NADH: cytochrome b5 reductase for activity. NAD 109-113 cytochrome b5 type A Homo sapiens 115-128 1964451-4 1990 An antibody against cytochrome b5 markedly reduced the CMP-NeuAc hydroxylase activity when added to incubation mixture containing either NADH or NADPH as an electron donor. NAD 137-141 cytochrome b5 type A Homo sapiens 20-33 2369123-2 1990 The reduction of exogenous cytochrome b5 by microsomes was low at 1.2 microM cytochrome b5 (3.9 or 2.7 nmol/min/mg protein, respectively, with NADH or NADPH). NAD 143-147 cytochrome b5 type A Homo sapiens 27-40 2369123-10 1990 In the presence of Triton X-100, divalent cations were inhibitory in NADH-dependent cytochrome b5 reduction, and in contrast, stimulative in NADPH-dependent reaction. NAD 69-73 cytochrome b5 type A Homo sapiens 84-97 2369123-11 1990 These findings suggest that the activation of cytochrome b5 reduction by divalent cations in the NADH system is mainly due to an increasing accessibility of the substrate, and in the NADPH system, in addition to this, a direct effect of divalent cations on NADPH-cytochrome P450 reductase is also involved. NAD 97-101 cytochrome b5 type A Homo sapiens 46-59 2369123-2 1990 The reduction of exogenous cytochrome b5 by microsomes was low at 1.2 microM cytochrome b5 (3.9 or 2.7 nmol/min/mg protein, respectively, with NADH or NADPH). NAD 143-147 cytochrome b5 type A Homo sapiens 77-90 2369123-6 1990 MgCl2 also stimulated cytochrome b5 reduction with a EC50 value of 1.0 mM in the NADH system or 0.6 mM in the NADPH system. NAD 81-85 cytochrome b5 type A Homo sapiens 22-35 2369123-8 1990 The Km value for cytochrome b5 was decreased and the Vmax was increased by calcium with either the NADH- or the NADPH-dependent system. NAD 99-103 cytochrome b5 type A Homo sapiens 17-30 2107882-7 1990 These observations suggest that replacement of Pro-127 causes a significant conformation change in the nucleotide-binding domain that affects electron transport from NADH to cytochrome b5. NAD 166-170 cytochrome b5 type A Homo sapiens 174-187 2459594-1 1988 Isolated and purified microsomal NADH-cytochrome b5 reductase (EC 1.6.2.2) was incubated with bleomycin (BLM) and FeCl3 in the presence of NADH. NAD 33-37 cytochrome b5 type A Homo sapiens 38-51 2459594-2 1988 Only when purified cytochrome b5 was added could an increased NADH consumption be observed indicating redox cycling of the BLM-Fe(III) complex. NAD 62-66 cytochrome b5 type A Homo sapiens 19-32 2459594-10 1988 The results reveal that the BLM-Fe(III) complex undergoes redox cycling by the microsomal NADH-dependent cytochrome b5 reductase-cytochrome b5 system. NAD 90-94 cytochrome b5 type A Homo sapiens 105-118 2459594-10 1988 The results reveal that the BLM-Fe(III) complex undergoes redox cycling by the microsomal NADH-dependent cytochrome b5 reductase-cytochrome b5 system. NAD 90-94 cytochrome b5 type A Homo sapiens 129-142 6972374-10 1981 It has been shown that the second electron for P-448(1) can also be supplied from NADH via cytochrome b5 in a reconstituted acetanilide p-hydroxylase system containing P-448(1), cytochrome b5, and the two reductases. NAD 82-86 cytochrome b5 type A Homo sapiens 91-104 3137923-0 1988 The opposite effect of bivalent cations on cytochrome b5 reduction by NADH:cytochrome b5 reductase and NADPH:cytochrome c reductase. NAD 70-74 cytochrome b5 type A Homo sapiens 43-56 3137923-0 1988 The opposite effect of bivalent cations on cytochrome b5 reduction by NADH:cytochrome b5 reductase and NADPH:cytochrome c reductase. NAD 70-74 cytochrome b5 type A Homo sapiens 75-88 3137923-1 1988 The effects of bivalent cations on cytochrome b5 reduction by NADH:cytochrome b5 reductase and NADPH:cytochrome c reductase were studied with the proteinase-solubilized enzymes. NAD 62-66 cytochrome b5 type A Homo sapiens 35-48 3137923-2 1988 Cytochrome b5 reduction by NADH:cytochrome b5 reductase was strongly inhibited by CaCl2 or MgCl2. NAD 27-31 cytochrome b5 type A Homo sapiens 0-13 3137923-2 1988 Cytochrome b5 reduction by NADH:cytochrome b5 reductase was strongly inhibited by CaCl2 or MgCl2. NAD 27-31 cytochrome b5 type A Homo sapiens 32-45 6699018-6 1984 Ninety per cent of the cytochrome b5 in the derivative was reduced with a first order rate constant of 51 s-1 upon the addition of NADH; the transfer of electrons from NADH to the reductase FAD prosthetic group, which is known to be the rate-limiting step in the reductase reaction mechanism, proceeded with an apparent rate constant of 57 s-1 under these conditions. NAD 131-135 cytochrome b5 type A Homo sapiens 23-36 6699018-6 1984 Ninety per cent of the cytochrome b5 in the derivative was reduced with a first order rate constant of 51 s-1 upon the addition of NADH; the transfer of electrons from NADH to the reductase FAD prosthetic group, which is known to be the rate-limiting step in the reductase reaction mechanism, proceeded with an apparent rate constant of 57 s-1 under these conditions. NAD 168-172 cytochrome b5 type A Homo sapiens 23-36 6811590-4 1982 In systems containing cytochrome and reductase, the rate of NADH oxidation exceeded that of NADPH oxidation, indicating that reduced cytochrome b5 is an effective electron donor for prostaglandin H2 formation, enhancing both the initial rate and the extent of the reaction. NAD 60-64 cytochrome b5 type A Homo sapiens 133-146 6216130-5 1982 These effects are both NAD+ and n-octylamine dependent and appear to be due to an activation of the microsomal enzyme causing endogenous reduction of NAD(P)+ and also, in part, to inhibition of the autooxidation of reduced cytochrome b5. NAD 23-27 cytochrome b5 type A Homo sapiens 223-236 7034720-1 1981 NADH--cytochrome b5 reductase and cytochrome b5 associated with slow-muscle sarcoplasmic reticulum and liver microsomal fraction were identified with discrete protein bands of molecular weights 33000 and 16700 by polyacrylamide-gel electrophoresis. NAD 0-4 cytochrome b5 type A Homo sapiens 6-19 7034720-1 1981 NADH--cytochrome b5 reductase and cytochrome b5 associated with slow-muscle sarcoplasmic reticulum and liver microsomal fraction were identified with discrete protein bands of molecular weights 33000 and 16700 by polyacrylamide-gel electrophoresis. NAD 0-4 cytochrome b5 type A Homo sapiens 34-47 6972374-9 1981 An electron flow from NADH via cytochrome b5 can be utilized as the second electron for the O-deethylase reaction of 7-ethoxycoumarin catalyzed by reconstituted systems containing P-450(2) and P-448(2) when both NADH-cytochrome b5 reductase and cytochrome b5 are included in the system, although the cytochrome has no stimulatory effect at all on the deethylase activity of these two cytochrome P-450"s. NAD 22-26 cytochrome b5 type A Homo sapiens 31-44 6972374-9 1981 An electron flow from NADH via cytochrome b5 can be utilized as the second electron for the O-deethylase reaction of 7-ethoxycoumarin catalyzed by reconstituted systems containing P-450(2) and P-448(2) when both NADH-cytochrome b5 reductase and cytochrome b5 are included in the system, although the cytochrome has no stimulatory effect at all on the deethylase activity of these two cytochrome P-450"s. NAD 22-26 cytochrome b5 type A Homo sapiens 217-230 6972374-9 1981 An electron flow from NADH via cytochrome b5 can be utilized as the second electron for the O-deethylase reaction of 7-ethoxycoumarin catalyzed by reconstituted systems containing P-450(2) and P-448(2) when both NADH-cytochrome b5 reductase and cytochrome b5 are included in the system, although the cytochrome has no stimulatory effect at all on the deethylase activity of these two cytochrome P-450"s. NAD 22-26 cytochrome b5 type A Homo sapiens 217-230 6326802-3 1984 The NAD+-bound reduced enzyme was oxidized by cytochrome b5 via the semiquinone intermediate. NAD 4-8 cytochrome b5 type A Homo sapiens 46-59 6326802-9 1984 A mechanism for electron transfer from NADH to cytochrome b5 is discussed on the basis of the one-electron redox potentials of the enzyme and is compared with the electron-transfer mechanism of NADPH-cytochrome P-450 reductase. NAD 39-43 cytochrome b5 type A Homo sapiens 47-60 7161259-6 1982 The synergistic effect with the addition of the NADH-linked electron transport system was more remarkable at the lower reduction levels of cytochrome b5 in the steady state. NAD 48-52 cytochrome b5 type A Homo sapiens 139-152 6275889-6 1982 NADH oxidation, both in intact and in water-treated mitochondria, is 90% inhibited by mersalyl, an inhibitor of the outer membrane NADH-cytochrome b5 reductase, and 10% inhibited by rotenone. NAD 0-4 cytochrome b5 type A Homo sapiens 136-149 6275889-10 1982 It is concluded that (i) oxidation of exogenous NADH in the presence of cytochrome c proceeds mostly through NADH-cytochrome b5 reductase and cytochrome b5 on the outer membrane and then through cytochrome oxidase via the cytochrome c shuttle, and (ii) ATP synthesis during oxidation of exogenous NADH is partly due to oxidation of endogenous substrates and partly to operation of cytochrome oxidase receiving electrons from the outer membrane via cytochrome c. NAD 48-52 cytochrome b5 type A Homo sapiens 114-127 6275889-10 1982 It is concluded that (i) oxidation of exogenous NADH in the presence of cytochrome c proceeds mostly through NADH-cytochrome b5 reductase and cytochrome b5 on the outer membrane and then through cytochrome oxidase via the cytochrome c shuttle, and (ii) ATP synthesis during oxidation of exogenous NADH is partly due to oxidation of endogenous substrates and partly to operation of cytochrome oxidase receiving electrons from the outer membrane via cytochrome c. NAD 48-52 cytochrome b5 type A Homo sapiens 142-155 6275889-10 1982 It is concluded that (i) oxidation of exogenous NADH in the presence of cytochrome c proceeds mostly through NADH-cytochrome b5 reductase and cytochrome b5 on the outer membrane and then through cytochrome oxidase via the cytochrome c shuttle, and (ii) ATP synthesis during oxidation of exogenous NADH is partly due to oxidation of endogenous substrates and partly to operation of cytochrome oxidase receiving electrons from the outer membrane via cytochrome c. NAD 109-113 cytochrome b5 type A Homo sapiens 114-127 7128914-0 1982 Nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate-dependent reduction of mammalian hepatic microsomal cytochrome b5: some properties of the enzyme system catalyzing the endogenous reduction of pyridine nucleotides. NAD 0-33 cytochrome b5 type A Homo sapiens 134-147 7128914-6 1982 The rates of reduction of cytochrome b5 and auto-oxidation of reduced cytochrome b5 were, however, much slower in NAD+ supplemented reaction media than in those supplemented with NADH. NAD 114-118 cytochrome b5 type A Homo sapiens 26-39 7128914-6 1982 The rates of reduction of cytochrome b5 and auto-oxidation of reduced cytochrome b5 were, however, much slower in NAD+ supplemented reaction media than in those supplemented with NADH. NAD 114-118 cytochrome b5 type A Homo sapiens 70-83 7128914-6 1982 The rates of reduction of cytochrome b5 and auto-oxidation of reduced cytochrome b5 were, however, much slower in NAD+ supplemented reaction media than in those supplemented with NADH. NAD 179-183 cytochrome b5 type A Homo sapiens 26-39 7128914-6 1982 The rates of reduction of cytochrome b5 and auto-oxidation of reduced cytochrome b5 were, however, much slower in NAD+ supplemented reaction media than in those supplemented with NADH. NAD 179-183 cytochrome b5 type A Homo sapiens 70-83 6265441-2 1981 During oxidation of exogenous NADH there is a fast and complete reduction of cytochrome b5 while endogenous or added exogenous cytochrome c become 10-15% and 100% reduced, respectively. NAD 30-34 cytochrome b5 type A Homo sapiens 77-90 6265441-3 1981 The reoxidation of cytochrome b5, after exhaustion of NADH, precedes that of cytochrome c. NAD 54-58 cytochrome b5 type A Homo sapiens 19-32 6265441-4 1981 NADH oxidation is blocked by mersalyl, an inhibitor of NADH-cytochrome b5 reductase. NAD 0-4 cytochrome b5 type A Homo sapiens 60-73 6265441-8 1981 It is concluded that aerobic oxidation of exogenous NADH involves the following pathway: NADH leads to NADH-cytochrome b5 reductase leads to cytochrome b5 leads to intermembrane cytochrome c leads to cytochrome oxidase leads to oxygen. NAD 52-56 cytochrome b5 type A Homo sapiens 108-121 6265441-8 1981 It is concluded that aerobic oxidation of exogenous NADH involves the following pathway: NADH leads to NADH-cytochrome b5 reductase leads to cytochrome b5 leads to intermembrane cytochrome c leads to cytochrome oxidase leads to oxygen. NAD 52-56 cytochrome b5 type A Homo sapiens 141-154 6265441-8 1981 It is concluded that aerobic oxidation of exogenous NADH involves the following pathway: NADH leads to NADH-cytochrome b5 reductase leads to cytochrome b5 leads to intermembrane cytochrome c leads to cytochrome oxidase leads to oxygen. NAD 89-93 cytochrome b5 type A Homo sapiens 108-121 6265441-8 1981 It is concluded that aerobic oxidation of exogenous NADH involves the following pathway: NADH leads to NADH-cytochrome b5 reductase leads to cytochrome b5 leads to intermembrane cytochrome c leads to cytochrome oxidase leads to oxygen. NAD 89-93 cytochrome b5 type A Homo sapiens 141-154 6972374-10 1981 It has been shown that the second electron for P-448(1) can also be supplied from NADH via cytochrome b5 in a reconstituted acetanilide p-hydroxylase system containing P-448(1), cytochrome b5, and the two reductases. NAD 82-86 cytochrome b5 type A Homo sapiens 178-191 7449761-0 1980 Direct enzyme titration curve of NADH: cytochrome b5 reductase by combined isoelectric focusing/electrophoresis. NAD 33-37 cytochrome b5 type A Homo sapiens 39-52 7449761-2 1980 Methemoglobin reduction in human red cells involves successively an electron transport from NADH to a soluble form of cytochrome b5 (step 1) and from cytochrome b5 to methemoglobin (step 2). NAD 92-96 cytochrome b5 type A Homo sapiens 118-131 7449761-3 1980 Step 1 is catalysed by an enzyme, soluble NADH:cytochrome b5 reductase (EC 1.6.2.2). NAD 42-46 cytochrome b5 type A Homo sapiens 47-60 235894-1 1975 A quantitative estimation of cytochrome b5 content in the NADPH- and NADH-oxidation chains. NAD 69-73 cytochrome b5 type A Homo sapiens 29-42 6246954-1 1980 Human placenta contains a thermostable, cytosolic NADH-diaphorase which is different from the other diaphorases and which we designate as diaphorase P. It is specific for NADH and reduces artificial substrates such as dichlorophenol and tetrazolium derivatives, but not natural substrates such as methemoglobin, cytochrome b5 or lipoate. NAD 50-54 cytochrome b5 type A Homo sapiens 312-325 19038-1 1977 Hepatic NADH-cytochrome b5 reductase was reduced by 1 mol of dithionite or NADH per mol of enzyme-bound FAD, without forming a stable semiquinone or intermediate during the titrations. NAD 8-12 cytochrome b5 type A Homo sapiens 13-26 19038-6 1977 Potentiometric titration of NADH-cytochrome b5 reductase at pH 7.0 with dithionite gave a midpoint potential of -258 mV; titration with NADH gave -160 mV. NAD 28-32 cytochrome b5 type A Homo sapiens 33-46 19038-6 1977 Potentiometric titration of NADH-cytochrome b5 reductase at pH 7.0 with dithionite gave a midpoint potential of -258 mV; titration with NADH gave -160 mV. NAD 136-140 cytochrome b5 type A Homo sapiens 33-46 167022-3 1975 When a small amount of NADH-cytochrome b5 reductase is bound liposomes simultaneously with cytochrome b5, the two proteins catalyze the reduction of cytochrome c by NADH. NAD 23-27 cytochrome b5 type A Homo sapiens 28-41 167022-3 1975 When a small amount of NADH-cytochrome b5 reductase is bound liposomes simultaneously with cytochrome b5, the two proteins catalyze the reduction of cytochrome c by NADH. NAD 23-27 cytochrome b5 type A Homo sapiens 91-104 239545-0 1975 Role of cytochrome b5 in NADPH-and NADH-dependent hydroxylation by the reconstituted cytochrome P-450- or P-448-containing system. NAD 35-39 cytochrome b5 type A Homo sapiens 8-21 199521-1 1977 Carboquone was found to greatly stimulate the aerobic NADH oxidation in the presence of both the partially purified NADH-cytochrome b5 reductase and cytochrome b5 prepared from hepatic microsomes by acting as an electron carrier from cytochrome b5 to molecular oxygen. NAD 54-58 cytochrome b5 type A Homo sapiens 121-134 239543-0 1975 Role of cytochrome b5 in the NADH synergism of NADPH-dependent reactions of the cytochrome P-450 monooxygenase system of hepatic microsomes. NAD 29-33 cytochrome b5 type A Homo sapiens 8-21 4374132-0 1974 Reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5 as electron carriers in NADH-supported cytochrome P-450 -dependent enzyme activities in liver microsomes. NAD 108-112 cytochrome b5 type A Homo sapiens 42-55 4156646-1 1974 Quantitative evaluation of the cytochrome b5 content in the NADPH and NADH oxidation chains]. NAD 70-74 cytochrome b5 type A Homo sapiens 31-44 4374132-0 1974 Reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5 as electron carriers in NADH-supported cytochrome P-450 -dependent enzyme activities in liver microsomes. NAD 108-112 cytochrome b5 type A Homo sapiens 70-83 4345437-0 1972 Interactions between NADH-cytochrome b5 reductase and cytochrome b5 preparations purified from liver microsomes. NAD 21-25 cytochrome b5 type A Homo sapiens 26-39 4366168-2 1974 The involvement of cytochrome b5 in the NADH-dependent hydroxylation of 3,4-benzpyrene by a reconstituted cytochrome P-448-containing system. NAD 40-44 cytochrome b5 type A Homo sapiens 19-32 4151403-0 1974 Immunochemical evidence for the participation of cytochrome b5 in the NADH synergism of the NADPH-dependent mono-oxidase system of hepatic microsomes. NAD 70-74 cytochrome b5 type A Homo sapiens 49-62 4345437-0 1972 Interactions between NADH-cytochrome b5 reductase and cytochrome b5 preparations purified from liver microsomes. NAD 21-25 cytochrome b5 type A Homo sapiens 54-67 33441761-6 2021 Further studies on cytochrome b5 (CYB5), an alternative NADH-dependent electron donor indicated particularly strong support of CYP2C8-dependent amodiaquine N-deethylation by CYB5 and this was confirmed by genetic CYB5 single- and POR/CYB5 double-knockout. NAD 56-60 cytochrome b5 type A Homo sapiens 19-32 33441761-6 2021 Further studies on cytochrome b5 (CYB5), an alternative NADH-dependent electron donor indicated particularly strong support of CYP2C8-dependent amodiaquine N-deethylation by CYB5 and this was confirmed by genetic CYB5 single- and POR/CYB5 double-knockout. NAD 56-60 cytochrome b5 type A Homo sapiens 34-38 33441761-6 2021 Further studies on cytochrome b5 (CYB5), an alternative NADH-dependent electron donor indicated particularly strong support of CYP2C8-dependent amodiaquine N-deethylation by CYB5 and this was confirmed by genetic CYB5 single- and POR/CYB5 double-knockout. NAD 56-60 cytochrome b5 type A Homo sapiens 174-178 33441761-6 2021 Further studies on cytochrome b5 (CYB5), an alternative NADH-dependent electron donor indicated particularly strong support of CYP2C8-dependent amodiaquine N-deethylation by CYB5 and this was confirmed by genetic CYB5 single- and POR/CYB5 double-knockout. NAD 56-60 cytochrome b5 type A Homo sapiens 174-178 33441761-6 2021 Further studies on cytochrome b5 (CYB5), an alternative NADH-dependent electron donor indicated particularly strong support of CYP2C8-dependent amodiaquine N-deethylation by CYB5 and this was confirmed by genetic CYB5 single- and POR/CYB5 double-knockout. NAD 56-60 cytochrome b5 type A Homo sapiens 174-178 33441761-8 2021 In summary our results show that POR/NADPH- and CYB5/NADH-electron transport systems influence human drug metabolizing CYPs differentially and differently than mouse Cyps. NAD 53-57 cytochrome b5 type A Homo sapiens 48-52 28497908-7 2017 The human and plants mARC proteins require a Cytochrome b5 (Cytb5) and a Cytochrome b5 reductase (Cytb5-R) to form an electron transfer chain from NADH to the NHC. NAD 147-151 cytochrome b5 type A Homo sapiens 45-58 31825806-1 2020 Cytochrome b5 reductase is an enzyme with the ability to generate superoxide anion at the expenses of NADH. NAD 102-106 cytochrome b5 type A Homo sapiens 0-13 31825806-6 2020 Upon complex formation with cytochrome b5 reductase, juglone is able to act as an electron acceptor leading to NADH consumption stimulation and increase of superoxide anion production by the reductase. NAD 111-115 cytochrome b5 type A Homo sapiens 28-41 30222979-1 2018 NADH cytochrome b5 reductase mediates electron transfer from NADH to cytochrome b5 utilizing flavin adenine dinucleotide as a redox cofactor. NAD 0-4 cytochrome b5 type A Homo sapiens 5-18 30222979-1 2018 NADH cytochrome b5 reductase mediates electron transfer from NADH to cytochrome b5 utilizing flavin adenine dinucleotide as a redox cofactor. NAD 0-4 cytochrome b5 type A Homo sapiens 69-82 28671819-0 2017 Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome b5/Cytochrome b5 Reductase/NADH System. NAD 91-95 cytochrome b5 type A Homo sapiens 53-66 28671819-0 2017 Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome b5/Cytochrome b5 Reductase/NADH System. NAD 91-95 cytochrome b5 type A Homo sapiens 67-80 28497908-7 2017 The human and plants mARC proteins require a Cytochrome b5 (Cytb5) and a Cytochrome b5 reductase (Cytb5-R) to form an electron transfer chain from NADH to the NHC. NAD 147-151 cytochrome b5 type A Homo sapiens 60-65 28497908-7 2017 The human and plants mARC proteins require a Cytochrome b5 (Cytb5) and a Cytochrome b5 reductase (Cytb5-R) to form an electron transfer chain from NADH to the NHC. NAD 147-151 cytochrome b5 type A Homo sapiens 73-86 28497908-7 2017 The human and plants mARC proteins require a Cytochrome b5 (Cytb5) and a Cytochrome b5 reductase (Cytb5-R) to form an electron transfer chain from NADH to the NHC. NAD 147-151 cytochrome b5 type A Homo sapiens 98-103 27372904-4 2016 We performed co-immunoprecipitation experiments to examine whether VILIP-3 can interact with reduced nicotine adenine dinucleotide (NADH)-cytochrome b 5 reductase. NAD 132-136 cytochrome b5 type A Homo sapiens 138-152 29104319-4 2017 We also evaluated the effectiveness of coenzymes of two of the microsomal reductases, NADPH as a coenzyme of POR, and NADH as a coenzyme of NADH:cytochrome b5 reductase, to mediate ellipticine oxidation in these enzyme systems. NAD 118-122 cytochrome b5 type A Homo sapiens 145-158 29104319-4 2017 We also evaluated the effectiveness of coenzymes of two of the microsomal reductases, NADPH as a coenzyme of POR, and NADH as a coenzyme of NADH:cytochrome b5 reductase, to mediate ellipticine oxidation in these enzyme systems. NAD 140-144 cytochrome b5 type A Homo sapiens 145-158 29104319-10 2017 In the presence of NADPH or NADH, cytochrome b5 stimulated the CYP3A4-mediated oxidation of ellipticine, but the stimulation effect differed for individual ellipticine metabolites. NAD 28-32 cytochrome b5 type A Homo sapiens 34-47 29104319-12 2017 The results demonstrate that cytochrome b5 plays a dual role in the CYP3A4-catalyzed oxidation of ellipticine: (1) cytochrome b5 mediates CYP3A4 catalytic activities by donating the first and second electron to this enzyme in its catalytic cycle, indicating that NADH:cytochrome b5 reductase can substitute NADPH-dependent POR in this enzymatic reaction and (2) cytochrome b5 can act as an allosteric modifier of the CYP3A4 oxygenase. NAD 263-267 cytochrome b5 type A Homo sapiens 29-42 29104319-12 2017 The results demonstrate that cytochrome b5 plays a dual role in the CYP3A4-catalyzed oxidation of ellipticine: (1) cytochrome b5 mediates CYP3A4 catalytic activities by donating the first and second electron to this enzyme in its catalytic cycle, indicating that NADH:cytochrome b5 reductase can substitute NADPH-dependent POR in this enzymatic reaction and (2) cytochrome b5 can act as an allosteric modifier of the CYP3A4 oxygenase. NAD 263-267 cytochrome b5 type A Homo sapiens 115-128 29104319-12 2017 The results demonstrate that cytochrome b5 plays a dual role in the CYP3A4-catalyzed oxidation of ellipticine: (1) cytochrome b5 mediates CYP3A4 catalytic activities by donating the first and second electron to this enzyme in its catalytic cycle, indicating that NADH:cytochrome b5 reductase can substitute NADPH-dependent POR in this enzymatic reaction and (2) cytochrome b5 can act as an allosteric modifier of the CYP3A4 oxygenase. NAD 263-267 cytochrome b5 type A Homo sapiens 115-128 29104319-12 2017 The results demonstrate that cytochrome b5 plays a dual role in the CYP3A4-catalyzed oxidation of ellipticine: (1) cytochrome b5 mediates CYP3A4 catalytic activities by donating the first and second electron to this enzyme in its catalytic cycle, indicating that NADH:cytochrome b5 reductase can substitute NADPH-dependent POR in this enzymatic reaction and (2) cytochrome b5 can act as an allosteric modifier of the CYP3A4 oxygenase. NAD 263-267 cytochrome b5 type A Homo sapiens 115-128 27575721-0 2016 Correction to NADH:Cytochrome b5 Reductase and Cytochrome b5 Can Act as Sole Electron Donors to Human Cytochrome P450 1A1-Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene. NAD 14-18 cytochrome b5 type A Homo sapiens 19-32 27575721-0 2016 Correction to NADH:Cytochrome b5 Reductase and Cytochrome b5 Can Act as Sole Electron Donors to Human Cytochrome P450 1A1-Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene. NAD 14-18 cytochrome b5 type A Homo sapiens 47-60 26466337-11 2015 The higher NADH-dependent cytochrome c reductase activity together with the higher transcript levels of CBR.1 and CYB5 in the crtR- mutant as well as the lower NADH-dependent activity in CBS-cbr.1- strongly suggest that CBR.1-CYB5 via participates as an alternative electron donor pathway for P450 enzymes involved in ergosterol biosynthesis in X. dendrorhous. NAD 11-15 cytochrome b5 type A Homo sapiens 114-118 27404282-0 2016 NADH:Cytochrome b5 Reductase and Cytochrome b5 Can Act as Sole Electron Donors to Human Cytochrome P450 1A1-Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene. NAD 0-4 cytochrome b5 type A Homo sapiens 5-18 27404282-0 2016 NADH:Cytochrome b5 Reductase and Cytochrome b5 Can Act as Sole Electron Donors to Human Cytochrome P450 1A1-Mediated Oxidation and DNA Adduct Formation by Benzo[a]pyrene. NAD 0-4 cytochrome b5 type A Homo sapiens 33-46 26466337-11 2015 The higher NADH-dependent cytochrome c reductase activity together with the higher transcript levels of CBR.1 and CYB5 in the crtR- mutant as well as the lower NADH-dependent activity in CBS-cbr.1- strongly suggest that CBR.1-CYB5 via participates as an alternative electron donor pathway for P450 enzymes involved in ergosterol biosynthesis in X. dendrorhous. NAD 11-15 cytochrome b5 type A Homo sapiens 226-230 23113554-4 2014 Cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. NAD 115-119 cytochrome b5 type A Homo sapiens 165-178 25446886-3 2015 Cyt-b5 can augment the 17,20-lyase activity of CYP17A1 by promoting the interaction of CYP17A1 and POR; enhance the 16-ene-synthase activity of CYP17A1 by acting as an electron donor; and enhance the activity of 3betaHSD by increasing the affinity of 3betaHSD for its cofactor NAD(+). NAD 277-283 cytochrome b5 type A Homo sapiens 0-6 23113554-4 2014 Cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. NAD 115-119 cytochrome b5 type A Homo sapiens 0-13 23228600-5 2013 We also review the recently published finding that cyt-b(5) allosterically augments the activity of 3beta-hydroxysteroid dehydrogenase/Delta(5)-Delta(4) isomerase (3betaHSD), a non cytochrome P450 enzyme, by increasing the enzymes affinity for its cofactor, NAD(+). NAD 258-264 cytochrome b5 type A Homo sapiens 51-59 23831226-1 2013 NADH-Cytochrome b5 reductase (b5R), a flavoprotein consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5 (Cb5). NAD 65-69 cytochrome b5 type A Homo sapiens 5-18 23831226-1 2013 NADH-Cytochrome b5 reductase (b5R), a flavoprotein consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5 (Cb5). NAD 65-69 cytochrome b5 type A Homo sapiens 216-229 23831226-1 2013 NADH-Cytochrome b5 reductase (b5R), a flavoprotein consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5 (Cb5). NAD 65-69 cytochrome b5 type A Homo sapiens 231-234 23831226-1 2013 NADH-Cytochrome b5 reductase (b5R), a flavoprotein consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5 (Cb5). NAD 0-4 cytochrome b5 type A Homo sapiens 5-18 23831226-1 2013 NADH-Cytochrome b5 reductase (b5R), a flavoprotein consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5 (Cb5). NAD 0-4 cytochrome b5 type A Homo sapiens 216-229 23831226-1 2013 NADH-Cytochrome b5 reductase (b5R), a flavoprotein consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5 (Cb5). NAD 0-4 cytochrome b5 type A Homo sapiens 231-234 23567315-1 2013 The microsomal NADH-dependent electron transport system consisting of cytochrome b5 reductase and cytochrome b5 participates in a number of physiologically important processes including lipid metabolism as well as is involved in the metabolism of various drug and xenobiotics. NAD 15-19 cytochrome b5 type A Homo sapiens 70-83 23567315-1 2013 The microsomal NADH-dependent electron transport system consisting of cytochrome b5 reductase and cytochrome b5 participates in a number of physiologically important processes including lipid metabolism as well as is involved in the metabolism of various drug and xenobiotics. NAD 15-19 cytochrome b5 type A Homo sapiens 98-111