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Article

Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins.

Proceedings of the National Academy of Sciences of the United States of America - 3 Aug 2010

Kruglik Sergei G, Yoo Byung-Kuk, Franzen Stefan, Vos Marten H, Martin Jean-Louis, Negrerie Michel

Abstract excerpt

We investigated the ultrafast structural transitions of the heme induced by nitric oxide (NO) binding for several heme proteins by subpicosecond time-resolved resonance Raman and femtosecond transient absorption spectroscopy. We probed the heme iron motion by the evolution of the iron-histidine Raman band intensity after NO photolysis. Unexpectedly, we found that the heme response and iron motion do not follow...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20643970
DOI: 10.1073/pnas.0912938107
PMCID: PMC2922218

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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