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Article

Cu(II)-binding properties of a cytochrome c with a synthetic metal-binding site: His-X3-His in an alpha-helix.

Proteins - 1 Jan 1991

Todd R J, Van Dam M E, Casimiro D, Haymore B L, Arnold F H

Abstract excerpt

A metal-binding site consisting of two histidines positioned His-X3-His in an alpha-helix has been engineered into the surface of Saccharomyces cerevisiae iso-1-cytochrome c. The synthetic metal-binding cytochrome c retains its biological activity in vivo. Its ability to bind chelated Cu(II) has...

Topics

Amino Acid Sequence
Base Sequence
Copper
Cytochrome c Group
Cytochromes c
Enzyme Stability
Genetic Variation
Histidine
Molecular Sequence Data
Protein Binding
Protein Conformation
Saccharomyces cerevisiae Proteins

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Identifiers

PMID: 1654548
DOI: 10.1002/prot.340100209

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1654548-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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