Effect of mutations of arginine 94 on proton pumping, electron transfer, and superoxide anion generation in cytochrome b of the bc1 complex from Rhodobacter sphaeroides.

Abstract excerpt

Proton transfer involving internal water molecules that provide hydrogen bonds and facilitate proton diffusion has been identified in some membrane proteins. Arg-94 in cytochrome b of the Rhodobacter sphaeroides bc(1) complex is fully conserved and is hydrogen-bonded to the heme propionate and a chain of water molecules. To further elucidate the role of Arg-94, we generated the mutations R94A, R94D, and R94N. The...

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