Conserved Met16 of Pseudoazurin Facilitates the Interprotein Electron Transfer to Copper-Containing Nitrite Reductase

Abstract Enzyme reaction of copper-containing nitrite reductase relies on the electron donor, pseudoazurin, yet the role of conserved pseudoazurin Met16 in electron transfer remains unclear. Combining cyclic voltammetry and stopped-flow kinetics, we show Met16 variants reduce kapp to 10–31 % of wild type and lower kcat/Km to 20–27%, indicating impaired complex formation and catalytic efficiency.

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Publication Details

Journal
Chemistry Letters
Published
2026-11-02
DOI
https://doi.org/10.1093/chemle/upag209
Primary Topic
Metalloenzymes and iron-sulfur proteins
Type
article
Field-Weighted Citation Impact
0.00
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article

Conserved Met16 of Pseudoazurin Facilitates the Interprotein Electron Transfer to Copper-Containing Nitrite Reductase

Airi Yamaguchi, Takahide Yamaguchi, Shota Hashimoto, Miwa Wakabayashi
Chemistry Letters
Metalloenzymes and iron-sulfur proteins
article

Conserved Met16 of Pseudoazurin Facilitates the Interprotein Electron Transfer to Copper-Containing Nitrite Reductase

Airi Yamaguchi, Takahide Yamaguchi, Shota Hashimoto, Miwa Wakabayashi
article en

Abstract

Abstract Enzyme reaction of copper-containing nitrite reductase relies on the electron donor, pseudoazurin, yet the role of conserved pseudoazurin Met16 in electron transfer remains unclear. Combining cyclic voltammetry and stopped-flow kinetics, we show Met16 variants reduce kapp to 10–31 % of wild type and lower kcat/Km to 20–27%, indicating impaired complex formation and catalytic efficiency.

Chemistry Letters
Ibaraki University (JP)
Openalex Percentile: Top 37%
Metalloenzymes and iron-sulfur proteins
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