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Article

Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.

Biochemistry - 7 Oct 2008

Maillett David H, Simplaceanu Virgil, Shen Tong-Jian, Ho Nancy T, Olson John S, Ho Chien

Abstract excerpt

Protein engineering strategies seek to develop a hemoglobin-based oxygen carrier with optimized functional properties, including (i) an appropriate O 2 affinity, (ii) high cooperativity, (iii) limited NO reactivity, and (iv) a diminished rate of auto-oxidation. The mutations alphaL29F, alphaL29W, alphaV96W and betaN108K individually impart some of these traits and in combinations produce hemoglobin molecules with...

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Identifiers

PMID: 18788751
DOI: 10.1021/bi800816v
PMCID: PMC2692483

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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