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Article

Neutron crystallography and quantum chemical analysis of bilin reductase PcyA mutants reveal substrate and catalytic residue protonation states.

The Journal of biological chemistry - 1 Jan 2023

Joutsuka Tatsuya, Nanasawa Ryota, Igarashi Keisuke, Horie Kazuki, Sugishima Masakazu, Hagiwara Yoshinori, Wada Kei, Fukuyama Keiichi, Yano Naomine, Mori Seiji, Ostermann Andreas, Kusaka Katsuhiro, Unno Masaki

Abstract excerpt

PcyA, a ferredoxin-dependent bilin pigment reductase, catalyzes the site-specific reduction of the two vinyl groups of biliverdin (BV), producing phycocyanobilin. Previous neutron crystallography detected both the neutral BV and its protonated form (BVH+) in the wildtype (WT) PcyA-BV complex, and a nearby catalytic residue Asp105 was found to have two conformations (protonated and deprotonated). Semiempirical...

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Identifiers

PMID: 36463961
DOI: 10.1016/j.jbc.2022.102763
PMCID: PMC9800206

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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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