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Valence tautomerism in synthetic models of cytochrome P450

Valence tautomerism in synthetic models of cytochrome P450

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4914151

Valence tautomerism in synthetic models of cytochrome P450

About this item

Full title

Valence tautomerism in synthetic models of cytochrome P450

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2016-06, Vol.113 (24), p.6611-6616

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

CytP450s have a cysteine-bound heme cofactor that, in its asisolated resting (oxidized) form, can be conclusively described as a ferric thiolate species. Unlike the native enzyme, most synthetic thiolate-bound ferric porphyrins are unstable in air unless the axial thiolate ligand is sterically protected. Spectroscopic investigations on a series of...

Alternative Titles

Full title

Valence tautomerism in synthetic models of cytochrome P450

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4914151

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4914151

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1600525113

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