PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15610027-0 2004 Characterization of the high-spin heme x in the cytochrome b6f complex of oxygenic photosynthesis. Heme 34-38 cytochrome b Chlamydomonas reinhardtii 48-60 15610027-6 2004 The pyridine hemochromagen redox difference spectrum for heme x covalently bound to the cytochrome b polypeptide isolated from SDS-PAGE displays a low-amplitude broad spectrum with a peak at 553 nm, similar to that of other hemes with a single thioether linkage. Heme 57-61 cytochrome b Chlamydomonas reinhardtii 88-100 15610027-6 2004 The pyridine hemochromagen redox difference spectrum for heme x covalently bound to the cytochrome b polypeptide isolated from SDS-PAGE displays a low-amplitude broad spectrum with a peak at 553 nm, similar to that of other hemes with a single thioether linkage. Heme 224-229 cytochrome b Chlamydomonas reinhardtii 88-100 15049703-1 2004 The three-dimensional structure of the cytochrome b(6)f complex disclosed the unexpected presence of a new heme c(i) [Stroebel, D., Choquet, Y., Popot, J.-L., and Picot, D. (2003) Nature 426, 413-418; Kurisu, G., Zhang, H., Smith, J. L., and Cramer, W. A. Heme 107-111 cytochrome b Chlamydomonas reinhardtii 39-51 15049703-4 2004 As predicted by the structure data, we identify a Cys(35)-containing proteolytic fragment (Tyr(25)-Lys(111)) from cytochrome b(6) as a peptide that covalently binds a heme. Heme 167-171 cytochrome b Chlamydomonas reinhardtii 114-126 11390403-0 2001 Photosynthetic water oxidation in cytochrome b(559) mutants containing a disrupted heme-binding pocket. Heme 83-87 cytochrome b Chlamydomonas reinhardtii 34-46 11390403-1 2001 The role of cytochrome b(559) in photosynthetic oxygen evolution has been investigated in three chloroplast mutants of Chlamydomonas reinhardtii, in which one of the two histidine axial ligands to the heme, provided by the alpha subunit, has been replaced by the residues methionine, tyrosine, and glutamine. Heme 201-205 cytochrome b Chlamydomonas reinhardtii 12-24 11390403-5 2001 Overall, these data establish unambiguously that a redox role for the heme of cytochrome b(559) is not required for photosynthetic oxygen evolution. Heme 70-74 cytochrome b Chlamydomonas reinhardtii 78-90 10681499-0 2000 On the spatial organization of hemes and chlorophyll in cytochrome b(6)f. A linear and circular dichroism study. Heme 31-36 cytochrome b Chlamydomonas reinhardtii 56-68 9405452-1 1997 Heme binding to cytochrome b6 is resistant, in part, to denaturing conditions that typically destroy the noncovalent interactions between the b hemes and their apoproteins, suggesting that one of two b hemes of holocytochrome b6 is tightly bound to the polypeptide. Heme 0-4 cytochrome b Chlamydomonas reinhardtii 16-28 9405452-1 1997 Heme binding to cytochrome b6 is resistant, in part, to denaturing conditions that typically destroy the noncovalent interactions between the b hemes and their apoproteins, suggesting that one of two b hemes of holocytochrome b6 is tightly bound to the polypeptide. Heme 144-149 cytochrome b Chlamydomonas reinhardtii 16-28 9405452-1 1997 Heme binding to cytochrome b6 is resistant, in part, to denaturing conditions that typically destroy the noncovalent interactions between the b hemes and their apoproteins, suggesting that one of two b hemes of holocytochrome b6 is tightly bound to the polypeptide. Heme 202-207 cytochrome b Chlamydomonas reinhardtii 16-28 17971335-8 2007 Sequence analysis revealed that HCF208 is a homolog of the Chlamydomonas reinhardtii CCB2 protein, which is a factor mediating attachment of heme c(n) to the cytochrome b(6) polypeptide as part of a novel heme biogenesis pathway, called system IV. Heme 141-145 cytochrome b Chlamydomonas reinhardtii 158-170 9637728-16 1998 In the proposed model for cytochrome b, both residues Tyr114 and Ser36 are in close proximity to the high-potential bH heme. Heme 119-123 cytochrome b Chlamydomonas reinhardtii 26-38