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. 1987 Dec 15;248(3):965–967. doi: 10.1042/bj2480965

Semisynthesis of cytochrome c analogues. The effect of modifying the conserved residues 38 and 39.

A E Proudfoot 1, C J Wallace 1
PMCID: PMC1148645  PMID: 2829847

Abstract

We have used chemical and enzymic protein engineering techniques to create analogues of the semisynthetic two-fragment complex (1-37).(38-104) of mitochondrial cytochrome c. This complex, unlike the natural product of specific tryptic cleavage, (1-38).(39-104), from which it is prepared, quite closely resembles the parent protein in functional characteristics and is thus a suitable substrate for modifications designed to study structure-function relations. We have replaced the invariant Arg-38 and the conserved Lys-39 with a range of alternative amino acids and have studied the effects on the principal functional parameters. The hydrogen-bonding capacity of Arg-38 is crucial to the stabilization of the bottom omega-loop, while the positive charge of Lys-39 helps maintain the high redox potential by electrostatic effects at the haem iron.

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Selected References

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