Cytochrome c oxidase: evidence for interaction of water molecules with cytochrome a.
The resonance Raman spectra of cytochrome c oxidase in protonated buffer compared to that in deuterated buffer indicate that water molecules are near the heme of cytochrome a. Differences in widths of the heme line at 1610 cm-1, after short exposure to D2O, and, additionally, of the heme line at 1625 cm-1, after long exposure, can be accounted for by changes in resonance vibrational energy transfer between modes of cytochrome a2+ and the bending mode of water molecules in the heme pocket. On the basis of the assignment of these modes, we place one water molecule near the vinyl group and one water molecule near the formyl group of the cytochrome a heme. These water molecules may play several possible functional roles.
Sassaroli
M
M
AT&T Bell Laboratories, Murray Hill, New Jersey 07974.
Ching
Y C
YC
Dasgupta
S
S
Rousseau
D L
DL
D000818:Animals; D001665:Binding Sites; D002021:Buffers; D002417:Cattle; D017936:Cytochrome a Group; D003580:Cytochromes; D003903:Deuterium; D017666:Deuterium Oxide; D004579:Electron Transport; D003576:Electron Transport Complex IV; D006418:Heme; D013059:Spectrum Analysis, Raman; D014867:Water
D002021:Buffers; D017936:Cytochrome a Group; D003580:Cytochromes; D014867:Water; D006418:Heme; D003903:Deuterium; D003576:Electron Transport Complex IV; D017666:Deuterium Oxide