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Article

Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64-->Thr variant.

The Biochemical journal - 15 May 1998

Maurus R, Bogumil R, Nguyen N T, Mauk A G, Brayer G

Abstract excerpt

The high-resolution X-ray crystallographic structures of horse heart azidometmyoglobin complexes of the wild-type protein and the His-64-->Thr variant have been determined to 2.0 and 1.8 A respectively. Azide binds to wild-type metmyoglobin in a bent configuration with an Fe-N-1-N-3 angle of 119 degrees and is oriented into the distal crevice in the direction of Ile-107. The proximity of the His-64 NE2 atom to...

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Identifiers

PMID: 9576852
DOI: 10.1042/bj3320067
PMCID: PMC1219452

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