PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2987042-1 1985 Stigmatellin, a chromone inhibitor acting at the Q0 center of the bc1 complex, binds to the heme b-566 domain of cytochrome b as well as to the Fe2S2 protein. Heme 92-96 mitochondrially encoded cytochrome b Homo sapiens 113-125 3011845-2 1986 Defects in the superoxide generating system were characterized at the level of the heme-containing cytochrome b and of the FAD-containing flavoprotein, both localized in the plasma membrane of granulocytes. Heme 83-87 mitochondrially encoded cytochrome b Homo sapiens 99-111 6322162-0 1984 Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane. Heme 157-162 mitochondrially encoded cytochrome b Homo sapiens 144-156 6086391-3 1984 The data strongly favor a cyclic redox loop mechanism in site 2 and show that either heme of the ferrous cytochrome b or ubisemiquinone formed in the QH2-oxidizing center of complex b-c1 is accessible to ferricyanide at the outer (M) side of the submitochondrial particle membrane. Heme 85-89 mitochondrially encoded cytochrome b Homo sapiens 105-117 166667-15 1975 When electron transfer from the b-type cytochromes to cytochrome C1, ubiquinone and duroquinone is inhibited by antimycin, the hemes of cytochrome b-566 and cytochrome b-562 (or cytochrome b-563 and cytochrome b-557) are in the reduced state. Heme 127-132 mitochondrially encoded cytochrome b Homo sapiens 136-148 16593381-1 1983 The two heme equivalents of cytochrome b-563 in the photosynthetic cytochrome b-f complex can be distinguished by their rate of reduction with dithionite at 25 degrees C and by their optical absorption spectra at 77 K. The cytochrome b component that is rapidly reduced after addition of dithionite or reduced ferredoxin possesses an alpha band that splits at 77 K into two peaks, at 557 and 561 nm. Heme 8-12 mitochondrially encoded cytochrome b Homo sapiens 67-79 16593381-1 1983 The two heme equivalents of cytochrome b-563 in the photosynthetic cytochrome b-f complex can be distinguished by their rate of reduction with dithionite at 25 degrees C and by their optical absorption spectra at 77 K. The cytochrome b component that is rapidly reduced after addition of dithionite or reduced ferredoxin possesses an alpha band that splits at 77 K into two peaks, at 557 and 561 nm. Heme 8-12 mitochondrially encoded cytochrome b Homo sapiens 67-79 16593381-1 1983 The two heme equivalents of cytochrome b-563 in the photosynthetic cytochrome b-f complex can be distinguished by their rate of reduction with dithionite at 25 degrees C and by their optical absorption spectra at 77 K. The cytochrome b component that is rapidly reduced after addition of dithionite or reduced ferredoxin possesses an alpha band that splits at 77 K into two peaks, at 557 and 561 nm. Heme 8-12 mitochondrially encoded cytochrome b Homo sapiens 28-40 221013-3 1979 The results show that the heme plane of cytochrome P-450 lies in the same plane as the membrane surface, whereas the cytochrome b5 heme plane has a random orientation. Heme 131-135 mitochondrially encoded cytochrome b Homo sapiens 117-129 30565588-1 2019 Engineered cytochrome b562, a small hemoprotein, with an externally-attached heme moiety via a moderately long linker at a suitable position predominantly forms a thermodynamically stable ring-shaped trimer in dilute solution. Heme 77-81 mitochondrially encoded cytochrome b Homo sapiens 11-23 31172469-2 2019 Referred to as cytochrome b558, because of its signature spectral absorbance at 558 nm in reduced-minus-oxidized difference spectroscopy, or cytochrome b(-245), because of its very low midpoint potential of -245 mV at pH 7.0, the protein possesses two stacked inequivalent hemes ligated by pairs of histidine residues in membrane helices h3 and h5. Heme 273-278 mitochondrially encoded cytochrome b Homo sapiens 15-27 30222979-6 2018 Using menadione as the substrate, quinone redox cycling was found to inhibit reduction of cytochrome b5 by cytochrome b5 reductase, as measured by heme spectral changes in cytochrome b5. Heme 147-151 mitochondrially encoded cytochrome b Homo sapiens 90-102 28493482-2 2017 In several prokaryotic lineages, and also in plant chloroplasts, the catalytic core of the cyt bc complexes is built of a four-helical cytochrome b (cyt b) that contains three hemes, a three-helical subunit IV, and an iron-sulfur Rieske protein (cytochrome b6 f-type complexes). Heme 176-181 mitochondrially encoded cytochrome b Homo sapiens 135-147 29240839-4 2017 We have analyzed the impact of interhelical loops on folding, assembly and stability of the heme-containing four-helix bundle transmembrane protein cytochrome b6 that is involved in charge transfer across biomembranes. Heme 92-96 mitochondrially encoded cytochrome b Homo sapiens 148-160 29240839-5 2017 Cytochrome b6 consists of two transmembrane helical hairpins that sandwich two heme molecules. Heme 79-83 mitochondrially encoded cytochrome b Homo sapiens 0-12 28493482-2 2017 In several prokaryotic lineages, and also in plant chloroplasts, the catalytic core of the cyt bc complexes is built of a four-helical cytochrome b (cyt b) that contains three hemes, a three-helical subunit IV, and an iron-sulfur Rieske protein (cytochrome b6 f-type complexes). Heme 176-181 mitochondrially encoded cytochrome b Homo sapiens 91-96 28493482-3 2017 In other prokaryotic lineages, and also in mitochondria, the cyt b subunit is fused with subunit IV, yielding a seven- or eight-helical cyt b with only two hemes (cyt bc1 -type complexes). Heme 156-161 mitochondrially encoded cytochrome b Homo sapiens 61-66 28493482-5 2017 This analysis provides further support to our earlier suggestion that (1) the ancestral version of cyt bc complex contained a small four-helical cyt b with three hemes similar to the plant cytochrome b6 and (2) independent fusion events led to the formation of large cyts b in several lineages. Heme 162-167 mitochondrially encoded cytochrome b Homo sapiens 99-104 26446353-3 2016 In this work, we propose a different interpretation of redox heterogeneity in the native population of Cyt b559 assuming redox interaction between the Cyt b559 heme group and a nearby bound quinone (Q). Heme 160-164 mitochondrially encoded cytochrome b Homo sapiens 103-108 28356734-6 2017 Using an optimized prokaryotic cell-free protein synthesis system, a recombinant cytochrome b558 containing functional hemes was produced and directly inserted into the lipid bilayer of specific liposomes. Heme 119-124 mitochondrially encoded cytochrome b Homo sapiens 81-93 28755362-4 2017 The Cytb 558 is the membrane catalytic core of the NADPH oxidase complex, through which the reducing equivalent provided by NADPH is transferred via the associated prosthetic groups (one flavin and two hemes) to reduce dioxygen into superoxide anion. Heme 202-207 mitochondrially encoded cytochrome b Homo sapiens 4-8 27108913-0 2016 Photo-induced oxidation of the uniquely liganded heme f in the cytochrome b6f complex of oxygenic photosynthesis. Heme 49-53 mitochondrially encoded cytochrome b Homo sapiens 63-75 26446353-3 2016 In this work, we propose a different interpretation of redox heterogeneity in the native population of Cyt b559 assuming redox interaction between the Cyt b559 heme group and a nearby bound quinone (Q). Heme 160-164 mitochondrially encoded cytochrome b Homo sapiens 151-156 26816006-0 2016 Peroxidase to Cytochrome b Type Transition in the Active Site of Heme-Bound Amyloid beta Peptides Relevant to Alzheimer"s Disease. Heme 65-69 mitochondrially encoded cytochrome b Homo sapiens 14-26 24498601-7 2013 Modeling showed that the p.C93Y mutation leads to disruption of the tertiary structure of Cytb by helix displacement, interfering with protein-heme interaction. Heme 143-147 mitochondrially encoded cytochrome b Homo sapiens 90-94 27025485-1 2016 A model of heme-quinone redox interaction has been developed for cytochrome b559 in photosystem II. Heme 11-15 mitochondrially encoded cytochrome b Homo sapiens 65-77 25723358-3 2015 Originally designed to mimic the bis-His cytochrome b, the Mimochrome structure was modified to introduce a peroxidase-like activity, by creating a distal cavity on the heme. Heme 169-173 mitochondrially encoded cytochrome b Homo sapiens 41-53 24841564-4 2014 Cytochrome b, a central catalytic subunit of complex III, contains two heme bs. Heme 71-75 mitochondrially encoded cytochrome b Homo sapiens 0-12 24841564-6 2014 Heme incorporation occurs in a strict sequential process that involves interactions of the newly synthesized cytochrome b with assembly factors and structural complex III subunits. Heme 0-4 mitochondrially encoded cytochrome b Homo sapiens 109-121 22890107-2 2012 Comparison of cytochrome b(6)f structures shows a variation in cytochrome f heme position that suggests the possibility of flexibility and motion of the extended cytochrome f structure that could entail a transient decrease in cluster-heme f distance. Heme 76-80 mitochondrially encoded cytochrome b Homo sapiens 14-26 22897206-0 2012 Heme binding constricts the conformational dynamics of the cytochrome b(559)" heme binding cavity. Heme 0-4 mitochondrially encoded cytochrome b Homo sapiens 59-71 22897206-0 2012 Heme binding constricts the conformational dynamics of the cytochrome b(559)" heme binding cavity. Heme 78-82 mitochondrially encoded cytochrome b Homo sapiens 59-71 22897206-1 2012 Cytochrome b(559)" is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding of a heme cofactor. Heme 137-141 mitochondrially encoded cytochrome b Homo sapiens 0-12 21315727-3 2011 We have analyzed the assembly and stability of the transmembrane cytochrome b(559)", which can be efficiently assembled in vitro from a heme-binding PsbF homo-dimer by combining free heme with the apo-cytochrome b(559)". Heme 136-140 mitochondrially encoded cytochrome b Homo sapiens 65-77 21315727-3 2011 We have analyzed the assembly and stability of the transmembrane cytochrome b(559)", which can be efficiently assembled in vitro from a heme-binding PsbF homo-dimer by combining free heme with the apo-cytochrome b(559)". Heme 136-140 mitochondrially encoded cytochrome b Homo sapiens 201-213 21315727-3 2011 We have analyzed the assembly and stability of the transmembrane cytochrome b(559)", which can be efficiently assembled in vitro from a heme-binding PsbF homo-dimer by combining free heme with the apo-cytochrome b(559)". Heme 183-187 mitochondrially encoded cytochrome b Homo sapiens 65-77 21315727-10 2011 Accordingly, the higher the pH value above 6-7, the more SDS is needed to improve heme binding, and this competes with the inherent tendency of SDS to dissociate cytochrome b(559)". Heme 82-86 mitochondrially encoded cytochrome b Homo sapiens 162-174 16963788-1 2006 We investigated the reactivity of heme-coordinating imidazole with diethylpyrocarbonate using a soluble domain of cytochrome b(5). Heme 34-38 mitochondrially encoded cytochrome b Homo sapiens 114-126 20630863-5 2010 Ncb5or is the first member of the cytochrome b(5) family shown to have such a heme environment. Heme 78-82 mitochondrially encoded cytochrome b Homo sapiens 34-46 19564403-3 2009 We demonstrate their association in a series of hetero-oligomeric complexes, some of which interact transiently with cytochrome b(6) in the process of heme delivery to the apoprotein. Heme 151-155 mitochondrially encoded cytochrome b Homo sapiens 117-129 17008316-2 2006 The quinol oxidase (Q(o)) site in this complex oxidizes a hydroquinone (quinol), reducing two one-electron carriers, a low potential cytochrome b heme and the "Rieske" iron-sulfur cluster. Heme 146-150 mitochondrially encoded cytochrome b Homo sapiens 133-145 17076484-0 2006 Heme-heme interactions in the cytochrome b6f complex: EPR spectroscopy and correlation with structure. Heme 0-4 mitochondrially encoded cytochrome b Homo sapiens 30-42 17076484-0 2006 Heme-heme interactions in the cytochrome b6f complex: EPR spectroscopy and correlation with structure. Heme 5-9 mitochondrially encoded cytochrome b Homo sapiens 30-42 19053119-1 2009 Supramolecular protein polymers: When a heme moiety was introduced to the surface of an apo-cytochrome b(562)(H63C) mutant, supramolecular polymers formed through noncovalent heme-heme pocket interactions. Heme 40-44 mitochondrially encoded cytochrome b Homo sapiens 92-104 19053119-1 2009 Supramolecular protein polymers: When a heme moiety was introduced to the surface of an apo-cytochrome b(562)(H63C) mutant, supramolecular polymers formed through noncovalent heme-heme pocket interactions. Heme 175-179 mitochondrially encoded cytochrome b Homo sapiens 92-104 19053119-1 2009 Supramolecular protein polymers: When a heme moiety was introduced to the surface of an apo-cytochrome b(562)(H63C) mutant, supramolecular polymers formed through noncovalent heme-heme pocket interactions. Heme 175-179 mitochondrially encoded cytochrome b Homo sapiens 92-104 18656488-1 2008 We have analyzed the role of individual heme-ligating histidine residues for assembly of holo-cytochrome b(6), and we show that the two hemes b(L) and b(H) bind in two subsequent steps to the apo-protein. Heme 40-44 mitochondrially encoded cytochrome b Homo sapiens 94-106 18656488-1 2008 We have analyzed the role of individual heme-ligating histidine residues for assembly of holo-cytochrome b(6), and we show that the two hemes b(L) and b(H) bind in two subsequent steps to the apo-protein. Heme 136-141 mitochondrially encoded cytochrome b Homo sapiens 94-106 18656488-6 2008 Furthermore, determination of the heme midpoint potentials of the various cytochrome b(6) variants indicates a cooperative adjustment of the heme midpoint potentials in cytochrome b(6). Heme 34-38 mitochondrially encoded cytochrome b Homo sapiens 74-86 18656488-6 2008 Furthermore, determination of the heme midpoint potentials of the various cytochrome b(6) variants indicates a cooperative adjustment of the heme midpoint potentials in cytochrome b(6). Heme 34-38 mitochondrially encoded cytochrome b Homo sapiens 169-181 18656488-6 2008 Furthermore, determination of the heme midpoint potentials of the various cytochrome b(6) variants indicates a cooperative adjustment of the heme midpoint potentials in cytochrome b(6). Heme 141-145 mitochondrially encoded cytochrome b Homo sapiens 74-86 18656488-6 2008 Furthermore, determination of the heme midpoint potentials of the various cytochrome b(6) variants indicates a cooperative adjustment of the heme midpoint potentials in cytochrome b(6). Heme 141-145 mitochondrially encoded cytochrome b Homo sapiens 169-181 18640599-9 2008 These distinct results might be related to a specific physiological mechanism being operative at the cytosolic heme center of cytochrome b(561). Heme 111-115 mitochondrially encoded cytochrome b Homo sapiens 126-138 17892950-3 2007 Cytochrome b6 can serve as an excellent model system for in vitro studies on the dynamic interplay of an apo-protein and heme cofactors during assembly of a transmembrane b-type cytochrome. Heme 121-125 mitochondrially encoded cytochrome b Homo sapiens 0-12 17892950-4 2007 In vitro assembled cytochrome b6 binds two hemes with different midpoint potentials and both ferri as well as ferro heme bind to the apo-cytochrome. Heme 43-48 mitochondrially encoded cytochrome b Homo sapiens 19-31 17892950-4 2007 In vitro assembled cytochrome b6 binds two hemes with different midpoint potentials and both ferri as well as ferro heme bind to the apo-cytochrome. Heme 43-47 mitochondrially encoded cytochrome b Homo sapiens 19-31 16939202-3 2006 The folding of cytochrome b(562), a four-helix-bundle heme protein, is hampered by heme dissociation. Heme 54-58 mitochondrially encoded cytochrome b Homo sapiens 15-27 16939202-4 2006 To overcome this complication, we have engineered a variant of cytochrome b(562) (cyt c-b(562)) featuring a c-type linkage between the heme and the polypeptide chain. Heme 135-139 mitochondrially encoded cytochrome b Homo sapiens 63-75 15032831-10 2004 The results are discussed in terms of different binding properties of the heme iron to the protonated or unprotonated histidine ligand in the high-potential and low-potential forms of cytochrome b(559), respectively. Heme 74-78 mitochondrially encoded cytochrome b Homo sapiens 184-196 15833348-3 2005 When the methionine-7 (Met-7) residue, which coordinates to the heme iron as an axial ligand, of the wild-type cytochrome b562 was replaced by an Ala or Gly residue, a water molecule bound to the heme iron and the electron transfer rate constants decreased to 1.3 x 10(-3) and 1.8 x 10(-3) cm s(-1), respectively. Heme 64-68 mitochondrially encoded cytochrome b Homo sapiens 111-123 15833348-3 2005 When the methionine-7 (Met-7) residue, which coordinates to the heme iron as an axial ligand, of the wild-type cytochrome b562 was replaced by an Ala or Gly residue, a water molecule bound to the heme iron and the electron transfer rate constants decreased to 1.3 x 10(-3) and 1.8 x 10(-3) cm s(-1), respectively. Heme 196-200 mitochondrially encoded cytochrome b Homo sapiens 111-123 15102859-4 2004 A remarkably high activity, over 100 micromol/s/micromol heme, was obtained in the oxidase with purified cyt b(558), ternary complex (p47-p67-p40(phox)), and Rac. Heme 57-61 mitochondrially encoded cytochrome b Homo sapiens 105-110 15102859-8 2004 The absorption spectra of reconstituted oxidase under anaerobiosis showed that incorporation of FAD into cyt b(558) recovered electron flow from NADPH to heme. Heme 154-158 mitochondrially encoded cytochrome b Homo sapiens 105-110 12729931-3 2003 The stability of Cyt b was enhanced in DDM relative to previously employed solubilizing agents as determined by both monitoring the heme spectrum in crude membrane extracts and assaying resistance to proteolytic degradation following purification. Heme 132-136 mitochondrially encoded cytochrome b Homo sapiens 17-22 14677976-1 2003 A HYSCORE investigation of the heme center in the cytochrome b(559) is presented. Heme 31-35 mitochondrially encoded cytochrome b Homo sapiens 50-62 12653566-0 2003 pH-induced alteration and oxidative destruction of heme in purified chromaffin granule cytochrome b(561): implications for the oxidative stress in catecholaminergic neurons. Heme 51-55 mitochondrially encoded cytochrome b Homo sapiens 87-99 12367526-3 2002 In particular, we have identified an area of significant sequence similarity between a three contiguous membrane-spanning domain of cytochrome b, which contains binding sites for two hemes, and a three contiguous membrane-spanning domain in the photosynthetic reaction center core subunits, which contains binding sites for cofactors such as (bacterio)chlorophylls, (bacterio)pheophytin and a non-heme iron. Heme 183-188 mitochondrially encoded cytochrome b Homo sapiens 132-144 12367526-3 2002 In particular, we have identified an area of significant sequence similarity between a three contiguous membrane-spanning domain of cytochrome b, which contains binding sites for two hemes, and a three contiguous membrane-spanning domain in the photosynthetic reaction center core subunits, which contains binding sites for cofactors such as (bacterio)chlorophylls, (bacterio)pheophytin and a non-heme iron. Heme 183-187 mitochondrially encoded cytochrome b Homo sapiens 132-144 12367526-4 2002 Three of the four heme ligands in cytochrome b are found to be conserved with the cofactor ligands in the reaction center polypeptides. Heme 18-22 mitochondrially encoded cytochrome b Homo sapiens 34-46 12136141-1 2002 Val45 is a highly conserved residue and a component of the heme-pocket wall of cytochrome b(5). Heme 59-63 mitochondrially encoded cytochrome b Homo sapiens 79-91 11771135-3 2001 If the main electrogenic stage of the Q cycle is suggested to be the electron transfer between the cytochrome b hemes, then the rate of superoxide generation sharply increases when delta psi grows from 150 mV to 180 mV. Heme 112-117 mitochondrially encoded cytochrome b Homo sapiens 99-111 11707449-5 2002 These findings indicate that the movement of the iron-sulfur subunit is composed of two discrete parts: a "micro-movement" at the cytochrome b interface, during which the [2Fe-2S] cluster interacts with ubihydroquinone oxidation site occupants and catalyzes ubihydroquinone oxidation, and a "macro-movement," during which the cluster domain swings away from cytochrome b interface, crosses the ef loop, and reaches a position close to cytochrome c(1) heme, to which it ultimately transfers an electron. Heme 451-455 mitochondrially encoded cytochrome b Homo sapiens 130-142 11707449-5 2002 These findings indicate that the movement of the iron-sulfur subunit is composed of two discrete parts: a "micro-movement" at the cytochrome b interface, during which the [2Fe-2S] cluster interacts with ubihydroquinone oxidation site occupants and catalyzes ubihydroquinone oxidation, and a "macro-movement," during which the cluster domain swings away from cytochrome b interface, crosses the ef loop, and reaches a position close to cytochrome c(1) heme, to which it ultimately transfers an electron. Heme 451-455 mitochondrially encoded cytochrome b Homo sapiens 358-370 11706033-7 2002 We also find that cytochrome b(5) minimally affects the heme active site of the enzyme, although both putidaredoxin and cytochrome b(5) bind to the same or similar site on P450(cam). Heme 56-60 mitochondrially encoded cytochrome b Homo sapiens 18-30 11106773-4 2000 The position of Cyt b(559) relative to Q(A) suggests that the heme plane is located on the stromal side of the thylakoid membrane. Heme 62-66 mitochondrially encoded cytochrome b Homo sapiens 16-21 11264014-4 2001 Heme dissociated from the reduced cyt b(5) protein at pH approximately 3.5, whereas its rate decreased under CO atmosphere compared with N(2) atmosphere, due to formation of a heme&bond;CO adduct with a histidine as an axial ligand. Heme 0-4 mitochondrially encoded cytochrome b Homo sapiens 34-41 11264014-4 2001 Heme dissociated from the reduced cyt b(5) protein at pH approximately 3.5, whereas its rate decreased under CO atmosphere compared with N(2) atmosphere, due to formation of a heme&bond;CO adduct with a histidine as an axial ligand. Heme 176-180 mitochondrially encoded cytochrome b Homo sapiens 34-41 11224519-3 2001 Electrons are initially transferred from NADPH to cytochrome b-associated FAD, then to cytochrome b heme and finally to molecular oxygen. Heme 100-104 mitochondrially encoded cytochrome b Homo sapiens 50-62 11224519-3 2001 Electrons are initially transferred from NADPH to cytochrome b-associated FAD, then to cytochrome b heme and finally to molecular oxygen. Heme 100-104 mitochondrially encoded cytochrome b Homo sapiens 87-99 11224519-6 2001 However, they must interact with each other to induce the subsequent transfer of electrons from FAD to cytochrome b heme and molecular oxygen. Heme 116-120 mitochondrially encoded cytochrome b Homo sapiens 103-115 11414837-1 2001 We generated atomic coordinates of an artificial protein that was recently synthesized to model the central part of the native cytochrome b (Cb) subunit consisting of a four-helix bundle with two hemes. Heme 196-201 mitochondrially encoded cytochrome b Homo sapiens 127-139 11414837-1 2001 We generated atomic coordinates of an artificial protein that was recently synthesized to model the central part of the native cytochrome b (Cb) subunit consisting of a four-helix bundle with two hemes. Heme 196-201 mitochondrially encoded cytochrome b Homo sapiens 141-143 11414837-5 2001 The model structure of the artificial Cb was used to determine the redox potentials of the two hemes by calculating the electrostatic energies from the solution of the linearized Poisson-Boltzmann equation (LPBE). Heme 95-100 mitochondrially encoded cytochrome b Homo sapiens 38-40 11414837-10 2001 For comparison and to test the computational procedure, the redox potentials of the two hemes in the native Cb from the cytochrome bc(1) (Cbc(1)) complex were also calculated. Heme 88-93 mitochondrially encoded cytochrome b Homo sapiens 108-110 11477221-0 2001 How does heme axial ligand deletion affect the structure and the function of cytochrome b(562)? Heme 9-13 mitochondrially encoded cytochrome b Homo sapiens 77-89 11477221-1 2001 We have recently generated a new mutant of cytochrome b(562) (cytb(562)) in which Met7, one of the axial heme ligands, is replaced by Ala (M7A cytb(562)). Heme 105-109 mitochondrially encoded cytochrome b Homo sapiens 43-55 11226432-1 2001 Low-temperature electron paramagnetic resonance (EPR) spectroscopy, circular dichroism and two-component redox titration have previously provided evidence for two different ascorbate-reducible heme centers in cytochrome b(561) present in chromaffin granule membranes. Heme 193-197 mitochondrially encoded cytochrome b Homo sapiens 209-221 11226432-6 2001 This species is either an alternative form of one of the hemes of cytochrome b(561) that has a very low redox potential or a b-type cytochrome distinct from b(561). Heme 57-62 mitochondrially encoded cytochrome b Homo sapiens 66-78 11018644-4 2000 Optical redox titrations of partially purified cytochrome b-561 indicated that it contains two hemes with similar spectral features, but distinct midpoint redox potentials (E(m7)+135 mV and +206 mV, respectively). Heme 95-100 mitochondrially encoded cytochrome b Homo sapiens 47-59 10986467-6 2000 The proximal and distal histidine sidechains coordinate directly to the heme iron, forming a hemichrome with spectral properties similar to those of cytochrome b(5). Heme 72-76 mitochondrially encoded cytochrome b Homo sapiens 149-161 10946110-4 2000 The specific requirement of reduced heme for in vitro synthesis of a cytochrome b(559)-derived holo-beta(2) suggests that cytochrome b synthesis in PSII might also be catalyzed in vivo. Heme 36-40 mitochondrially encoded cytochrome b Homo sapiens 69-81 10852709-1 2000 A Model-Free analysis of the (15)N relaxation properties of oxidized cytochrome b(5), a heme-containing electron-transfer protein, has been performed in 2 M guanidinium chloride (GdmCl), i.e., just before the heme is released by the action of denaturant. Heme 88-92 mitochondrially encoded cytochrome b Homo sapiens 69-81 10852709-1 2000 A Model-Free analysis of the (15)N relaxation properties of oxidized cytochrome b(5), a heme-containing electron-transfer protein, has been performed in 2 M guanidinium chloride (GdmCl), i.e., just before the heme is released by the action of denaturant. Heme 209-213 mitochondrially encoded cytochrome b Homo sapiens 69-81 10946110-4 2000 The specific requirement of reduced heme for in vitro synthesis of a cytochrome b(559)-derived holo-beta(2) suggests that cytochrome b synthesis in PSII might also be catalyzed in vivo. Heme 36-40 mitochondrially encoded cytochrome b Homo sapiens 122-134 9695291-6 1998 METHODS AND RESULTS: The difference of the reduced minus oxidized cyt b558 spectrum was measured under no interference from oxy Hb at the alpha and beta bands and differentiated as d[delta A]/d lambda (lambda = wavelength) to obtain further evidence for the defects of the cyt b558 heme spectrum. Heme 282-286 mitochondrially encoded cytochrome b Homo sapiens 66-71 10591529-4 1999 When the midpoint potential of the Rieske cluster is more positive than that of the heme of cytochrome c1, reduction of cytochrome b is biphasic. Heme 84-88 mitochondrially encoded cytochrome b Homo sapiens 120-132 9668203-2 1998 Assuming that electron transfer between hemes of cytochrome b is the main electrogenic step of the Q-cycle, we found that rate of superoxide production increased dramatically with increase in DeltaPsi in the range from 170 to 200 mV. Heme 41-46 mitochondrially encoded cytochrome b Homo sapiens 50-62 9568902-1 1998 Cytochrome b562 is a four-helix-bundle protein containing a non-covalently bound b-type heme prosthetic group. Heme 88-92 mitochondrially encoded cytochrome b Homo sapiens 0-12 9405047-0 1997 Energetics of heme binding to native and denatured states of cytochrome b562. Heme 14-18 mitochondrially encoded cytochrome b Homo sapiens 61-73 9405047-1 1997 Cytochrome b562 is a four-helix bundle protein containing a noncovalently bound b-type heme prosthetic group. Heme 87-91 mitochondrially encoded cytochrome b Homo sapiens 0-12 9131041-2 1997 Cytochrome b-559 bears the NADPH binding site and the redox centers (FAD and heme). Heme 77-81 mitochondrially encoded cytochrome b Homo sapiens 0-12 9341176-3 1997 The role of heme in cytochrome b558 biosynthesis was studied using succinyl acetone, an inhibitor of heme synthesis, in PLB-985 myeloid cells undergoing granulocytic differentiation. Heme 12-16 mitochondrially encoded cytochrome b Homo sapiens 20-32 9533030-5 1997 Histidine residues, which are possible heme axial ligands in cytochrome b of complex II, were found in the second transmembrane segment of each subunit. Heme 39-43 mitochondrially encoded cytochrome b Homo sapiens 61-73 9080180-1 1996 BACKGROUND: Cytochrome B562 is a heme-containing, four-helix bundle. Heme 33-37 mitochondrially encoded cytochrome b Homo sapiens 12-24 8885841-0 1996 Bis-methionine ligation to heme iron in mutants of cytochrome b562. Heme 27-31 mitochondrially encoded cytochrome b Homo sapiens 51-63 8885841-3 1996 We have generated mutants of cytochrome b562 in which the histidine ligand to the heme iron (His102) has been replaced by a methionine. Heme 82-86 mitochondrially encoded cytochrome b Homo sapiens 29-41 8885842-0 1996 Bis-methionine ligation to heme iron in mutants of cytochrome b562. Heme 27-31 mitochondrially encoded cytochrome b Homo sapiens 51-63 8885842-3 1996 Previous work has shown that, in variants of cytochrome b562 containing the H102M mutation, methionine residues provide both axial ligands to the heme iron. Heme 146-150 mitochondrially encoded cytochrome b Homo sapiens 45-57 8885842-6 1996 We have used one and two dimensional, homonuclear NMR spectroscopy to assign the proton resonances of the heme group and ligand side chains in the reduced, cytochrome b562 variants, H102M and covR98C/H102M. Heme 106-110 mitochondrially encoded cytochrome b Homo sapiens 156-168 8654562-0 1996 Correlated behavior of the EPR signal of cytochrome b-559 heme Fe(III) ligated by OH- and the multiline signal of the Mn cluster in PS-II membrane fragments. Heme 58-62 mitochondrially encoded cytochrome b Homo sapiens 41-53 8654562-4 1996 These results are discussed in terms of the light-induced formation of a bound OH" radical shared between the Cyt b-559 heme Fe and the Mn cluster as a first step of water oxidation. Heme 120-124 mitochondrially encoded cytochrome b Homo sapiens 110-115 8549748-0 1995 Study of heme Fe(III) ligated by OH- in cytochrome b-559 and its low temperature photochemistry in intact chloroplasts. Heme 9-13 mitochondrially encoded cytochrome b Homo sapiens 40-52 8549752-0 1995 Spectroscopic identification of the heme axial ligation of cytochrome b558 in the NADPH oxidase of porcine neutrophils. Heme 36-40 mitochondrially encoded cytochrome b Homo sapiens 59-71 8549752-1 1995 The combination of electron paramagnetic resonance (EPR), near-infrared magnetic circular dichroism (NIR-MCD) and resonance Raman (RR) spectroscopies at cryogenic temperatures has been used to identify the axial heme ligation of the low spin cytochrome b558 component of NADPH oxidase from porcine blood neutrophils. Heme 212-216 mitochondrially encoded cytochrome b Homo sapiens 242-254 30897680-0 1996 Influence of KF, DCMU and removal of Ca+ on the high-spin EPR signal of the cytochrome b-559 heme Fe(III) ligated by OH- in chloroplasts. Heme 93-97 mitochondrially encoded cytochrome b Homo sapiens 76-88 1332761-10 1992 The excellent agreement between model compounds and isolated Cyt b559 reinforces the validity of the model of a heme iron coordinated to two histidine residues for Cyt b559. Heme 112-116 mitochondrially encoded cytochrome b Homo sapiens 61-66 7713877-1 1995 Phagocytic cytochrome b558 is a unique heme-containing enzyme, which catalyzes one electron reduction of molecular oxygen to produce a superoxide anion with a six-coordinated heme iron. Heme 39-43 mitochondrially encoded cytochrome b Homo sapiens 11-23 7713877-1 1995 Phagocytic cytochrome b558 is a unique heme-containing enzyme, which catalyzes one electron reduction of molecular oxygen to produce a superoxide anion with a six-coordinated heme iron. Heme 175-179 mitochondrially encoded cytochrome b Homo sapiens 11-23 7726562-6 1995 In the purified bc1 complex, DBHBM and antimycin A induced a red shift from 562 to 566 nm of the alpha peak of cytochrome b, supporting the idea that DBHBM influences predominantly the ligand field of the b562 (bh) heme. Heme 215-219 mitochondrially encoded cytochrome b Homo sapiens 111-123 7896790-6 1995 Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen. Heme 317-321 mitochondrially encoded cytochrome b Homo sapiens 325-337 7615499-0 1995 Cytochrome b-245 of the neutrophil superoxide-generating system contains two nonidentical hemes. Heme 90-95 mitochondrially encoded cytochrome b Homo sapiens 0-12 8307196-7 1994 A kinetic study of O2- production by cytochrome b559 reflavinated under stoichiometric FAD binding conditions revealed an FAD/heme ratio of 1:2. Heme 126-130 mitochondrially encoded cytochrome b Homo sapiens 37-49 1320378-7 1992 Cytochrome b-245 appears to bind both the haem and FAD, in a molar ratio of 2:1. Heme 42-46 mitochondrially encoded cytochrome b Homo sapiens 0-12 1559974-0 1992 Human neutrophil cytochrome b contains multiple hemes. Heme 48-53 mitochondrially encoded cytochrome b Homo sapiens 17-29 1559974-8 1992 Our current results indicate that human neutrophil cytochrome b is a bi-heme or possibly tri-heme molecule with at least one heme residing in the large subunit and one shared between both subunits and that the heme-containing regions of the cytochrome probably lie within the membrane lipid bilayer. Heme 72-76 mitochondrially encoded cytochrome b Homo sapiens 51-63 1559974-8 1992 Our current results indicate that human neutrophil cytochrome b is a bi-heme or possibly tri-heme molecule with at least one heme residing in the large subunit and one shared between both subunits and that the heme-containing regions of the cytochrome probably lie within the membrane lipid bilayer. Heme 93-97 mitochondrially encoded cytochrome b Homo sapiens 51-63 1332761-14 1992 The differences observed in the amplitude of the 1660/1652-cm-1 band, at 1700 and 1530-1510 cm-1 in the light-induced FTIR difference spectra of Cyt b559 HP and LP, show that the mechanisms of heme oxidation in vivo imply different molecular processes for the two forms Cyt b559 HP and LP. Heme 193-197 mitochondrially encoded cytochrome b Homo sapiens 145-150 1332761-14 1992 The differences observed in the amplitude of the 1660/1652-cm-1 band, at 1700 and 1530-1510 cm-1 in the light-induced FTIR difference spectra of Cyt b559 HP and LP, show that the mechanisms of heme oxidation in vivo imply different molecular processes for the two forms Cyt b559 HP and LP. Heme 193-197 mitochondrially encoded cytochrome b Homo sapiens 270-275 2836381-3 1988 The results are in favor of two independent quinone binding sites at opposite surfaces of the membrane, topping one of the two hemes of cytochrome b each. Heme 127-132 mitochondrially encoded cytochrome b Homo sapiens 136-148 1732158-4 1992 The 15257 mutation altered a highly conserved amino acid in an extramembrane domain of cytochrome b that is associated with the ligation of the low potential b566 heme and the 5244 mutation altered a strongly evolutionarily conserved region of the ND2 polypeptide. Heme 163-167 mitochondrially encoded cytochrome b Homo sapiens 87-99 2538154-3 1989 Spectroscopic characterization of these two species revealed that the 47 kDa protein binds chlorophyll a, whereas the D1-D2-cytochrome b-559 complex shows an enrichment in Pheo a and heme on a chlorophyll basis. Heme 183-187 mitochondrially encoded cytochrome b Homo sapiens 124-136 2909509-1 1989 We have attempted to purify the heme moiety of cytochrome b558 from human neutrophils. Heme 32-36 mitochondrially encoded cytochrome b Homo sapiens 47-59 2909509-8 1989 The amino acid composition of the heme-containing moiety of cytochrome b558 was abundant in hydrophobic amino acids. Heme 34-38 mitochondrially encoded cytochrome b Homo sapiens 60-72 2909509-11 1989 These results indicate that this method provides the purification of the small subunit of human cytochrome b558 which is the heme-carrying subunit of cytochrome b558, and suggest that cytochrome b558 has heme-heme interaction and some conformational changes in the alternation of the redox state. Heme 125-129 mitochondrially encoded cytochrome b Homo sapiens 96-108 2909509-11 1989 These results indicate that this method provides the purification of the small subunit of human cytochrome b558 which is the heme-carrying subunit of cytochrome b558, and suggest that cytochrome b558 has heme-heme interaction and some conformational changes in the alternation of the redox state. Heme 204-208 mitochondrially encoded cytochrome b Homo sapiens 96-108 2909509-11 1989 These results indicate that this method provides the purification of the small subunit of human cytochrome b558 which is the heme-carrying subunit of cytochrome b558, and suggest that cytochrome b558 has heme-heme interaction and some conformational changes in the alternation of the redox state. Heme 204-208 mitochondrially encoded cytochrome b Homo sapiens 96-108 1846361-1 1991 The resonance Raman spectra of neutrophil cytochrome b558 obtained upon Soret excitation indicate that the heme is low spin six-coordinate in both ferric and ferrous oxidation states; comparison with the spectra of bis-imidazole hemin suggests imidazole or imidazolate axial ligation. Heme 107-111 mitochondrially encoded cytochrome b Homo sapiens 42-54 1846361-5 1991 Midpoint reduction potentials and resonance Raman spectra of the soluble cytochrome b558 from an individual with cytochrome b558 positive (type IA.2) chronic granulomatous disease were nearly identical to normal oxidase, with the exception that the deficient oxidase did not undergo heme photoreduction. Heme 283-287 mitochondrially encoded cytochrome b Homo sapiens 73-85 24429768-4 1988 Resolution of the properties of the two cytochrome b 6 hemes has relied upon the availability of purified solubilized complex, while evidence in the thylakoid suggests the difference between the two hemes are not as great in situ. Heme 55-60 mitochondrially encoded cytochrome b Homo sapiens 40-52 3337799-9 1988 Experiments aimed at identifying the heme-carrying subunit(s) were inconclusive, since dissociation of the complex resulted in loss of cytochrome b spectrum. Heme 37-41 mitochondrially encoded cytochrome b Homo sapiens 135-147 3818601-4 1987 Based upon current models for the secondary structure of cytochrome b, the altered amino acid lies in close proximity to one of the invariant histidine residues involved in binding the heme groups. Heme 185-189 mitochondrially encoded cytochrome b Homo sapiens 57-69