PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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reinhardtii, in which one of the two histidine axial ligands to the heme, provided by the alpha subunit, has been replaced by the residues methionine, tyrosine, and glutamine.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	
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	
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