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Article

Redox properties of wild-type and heme-binding loop mutants of bacterial cytochromes C measured by direct electrochemistry.

Inorganic chemistry - 28 Nov 2005

Ye Tao, Kaur Ravinder, Wen Xin, Bren Kara L, Elliott Sean J

Abstract excerpt

We have used protein film voltammetry (PFV) to determine the midpoint potentials of the Pseudomonas aeruginosa, Hydrogenobacter thermophilus, and Nitrosomonas europaea wild-type monoheme cytochromes c (cyts c; PA, HT, and NE, respectively), as well as PA N64Q, HT Q64N, and NE V65delta mutants, as a function of pH, and buffer conditions. Recent studies have suggested that the identity of the 64 position of the...

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PMID: 16296855
DOI: 10.1021/ic051003l

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