title: Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition.
abstract: We found that cyt c Y67H and Y67R variants represent a state which resembles the conformational intermediate state in cyt c with high peroxidase activity; and also the hydrogen bond network around Tyr67 is associated with the conformational transition of cyt c; these suggest that the hydrogen bond network around Tyr67 is essential in maintaining the cyt c functioning not only as an electron transfer protein but also probably as a trigger in apoptosis.
authors.affiliation: Department of Chemistry & Institutes of Biomedical Sciences, Fudan University, Shanghai 200433, China.
authors.forename: Tianlei
authors.initials: T
authors.lastname: Ying
authors.forename: Zhong-Hua
authors.initials: ZH
authors.lastname: Wang
authors.forename: Ying-Wu
authors.initials: YW
authors.lastname: Lin
authors.forename: Jin
authors.initials: J
authors.lastname: Xie
authors.forename: Xiangshi
authors.initials: X
authors.lastname: Tan
authors.forename: Zhong-Xian
authors.initials: ZX
authors.lastname: Huang
mesh_terms: D017209:Apoptosis / Q000502:physiology*; D045304:Cytochromes c / Q000737:chemistry* / Q000502:physiology*; D004579:Electron Transport; D006860:Hydrogen Bonding; D011487:Protein Conformation; D014443:Tyrosine / Q000737:chemistry*
chemical_list: D014443:Tyrosine; D045304:Cytochromes c