High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase.

doi:10.1016/j.jmb.2005.04.006

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Article

High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase.

Journal of molecular biology - 8 Jul 2005

Hough Michael A, Ellis Mark J, Antonyuk Svetlana, Strange Richard W, Sawers Gary, Eady Robert R, Samar Hasnain S

Abstract excerpt

We present high-resolution crystal structures and functional analysis of T1Cu centre mutants of nitrite reductase that perturb the redox potential and the Cys130-His129 "hard-wired" bridge through which electron transfer to the catalytic T2Cu centre occurs. These data provide insight into how activity can be altered through mutational manipulation of the electron delivery centre (T1Cu). The alteration of Cys to...

Topics

Achromobacter denitrificans
Anisotropy
Azurin
Catalysis
Copper
Crystallization
Crystallography, X-Ray
Electron Spin Resonance Spectroscopy
Electron Transport
Ligands
Models, Molecular
Mutation
Nitrite Reductases

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Static Electricity

Structure-Activity Relationship

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Open in PubMed

Identifiers

PMID: 15927201
DOI: 10.1016/j.jmb.2005.04.006

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