Model studies on the active site of cytochrome P-450: An FeII-porphyrin carrying a strapped thiolate ligand

Alan R. Battersby, William Howson, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

An FeII-porphyrin has been synthesised with a strap carrying a thiolate residue covalently bound across one face of the macrocycle; the spectroscopic properties of the carbon monoxide complex of this model system closely match those of the CO-complex of cytochrome P-450.

Original languageEnglish (US)
Pages (from-to)1266-1268
Number of pages3
JournalJournal of the Chemical Society D: Chemical Communications
Issue number21
DOIs
StatePublished - 1982

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Porphyrins
Carbon Monoxide
Carbon monoxide
Cytochrome P-450 Enzyme System
Catalytic Domain
Ligands

ASJC Scopus subject areas

  • Molecular Medicine

Cite this

Model studies on the active site of cytochrome P-450 : An FeII-porphyrin carrying a strapped thiolate ligand. / Battersby, Alan R.; Howson, William; Hamilton, Andrew.

In: Journal of the Chemical Society D: Chemical Communications, No. 21, 1982, p. 1266-1268.

Research output: Contribution to journalArticle

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