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Small weak acids stimulate proton transfer events in site‐directed mutants of the two ionizable residues, Glu L212 and Asp L213 , in the Q B ‐binding site of Rhodobacter sphaeroides reaction center
Author(s) -
Takahashi Eiji,
Wraight Colin A.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80572-k
Subject(s) - chemistry , proton , mutant , stereochemistry , binding site , crystallography , biochemistry , physics , quantum mechanics , gene
Mutations of the two ionizable residues. Glu L212 and Asp L213 , in the secondary quinone (Q # ) binding site of reaction centers (RCs) from Rhodobacter sphaeroides cause major dysfunctions in the proton transfer processes leading to the formation of quinol. Mutant RCs with Asp L213 → Asn are especially severely blocked, and the rate of the proton‐limited transfer of the second electron is at least IO 4 times slower than in the wild‐type. Small, weak acids, such as azide/hydrazoic acid (N 3 − /HN 3 ; pϰ ∼ 4.7) accelerated the electron transfer rate in mutant RCs in a pH and concentration‐dependent manner, consistent with their functioning as protein‐penetrating protonophores, delivering protons to the Q # site in a non‐specific, diffusive process. Other small weak acids similarly with efficacies dependent on their size and pϰ values. In terms of the concentration of protonated species, the relative effectiveness was: nitrite > cyanate & sim; formate > azide > > acetate. The behavior of bacterial RCs containing the Asp L213 → Asn mutation resembles that of bicarbonate‐depleted photosystem II, and the mutational block is partially alleviated by bicarbonate. The possibility is discussed that bicarbonate acts in PS II as an analogue to the carboxylic acid residues of the bacterial proton conduction pathway.