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Article

Bioluminescence is produced from a trapped firefly luciferase conformation predicted by the domain alternation mechanism.

Journal of the American Chemical Society - 27 Jul 2011

Branchini Bruce R, Rosenberg Justin C, Fontaine Danielle M, Southworth Tara L, Behney Curran E, Uzasci Lerna

Abstract excerpt

According to the domain alternation mechanism and crystal structure evidence, the acyl-CoA synthetases, one of three subgroups of a superfamily of adenylating enzymes, catalyze adenylate- and thioester-forming half-reactions in two different conformations. The enzymes accomplish this by presenting two active sites through an ~140° rotation of the C-domain. The second half-reaction catalyzed by another subgroup,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 21707059
DOI: 10.1021/ja2041496

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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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