Editing Cytochrome c (section)

=== Heme c ===

[[File:Heme c.svg|thumb|Structure of heme c]]

While most heme proteins are attached to the prosthetic group through iron ion ligation and tertiary interactions, the heme group of cytochrome c makes thioether bonds with two [[cysteine]] side chains of the protein.<ref>{{Cite journal |vauthors=Kang X, Carey J |date=November 1999 |title=Role of heme in structural organization of cytochrome c probed by semisynthesis |journal=[[Biochemistry (journal)|Biochemistry]] |volume=38 |issue=48 |pages=15944–51 |doi=10.1021/bi9919089 |pmid=10625461}}</ref> One of the main properties of heme c, which allows cytochrome c to have variety of functions, is its ability to have different reduction potentials in nature. This property determines the kinetics and thermodynamics of an electron transfer reaction.<ref>{{Cite journal |vauthors=Zhao Y, Wang ZB, Xu JX |date=January 2003 |title=Effect of cytochrome c on the generation and elimination of O{{sub|2}}{{sup|–}} and H{{sub|2}}O{{sub|2}} in mitochondria |journal=[[The Journal of Biological Chemistry]] |volume=278 |issue=4 |pages=2356–60 |doi=10.1074/jbc.M209681200 |pmid=12435729 |doi-access=free}}</ref>