Abstract 1534 Dissecting the Roles of Periplasmic Nitrate Reductase Structural Components and Their Impact on Molybdenum Cofactor Reactivity

The reduction of nitrate by Campylobacter jejuni is catalyzed by a periplasmic nitrate reductase (Nap) complex. The catalytic subunit, NapA, harbors a molybdenum center where catalysis takes place. The catalysis relies on the molybdenum cofactor (Moco) that has a pterin-bound molybdenum center and a partner prosthetic group, an iron-sulfur cluster. Electrons are transferred to NapA during the reduction of nitrate by a second subunit called NapB, which contains diheme cytochrome c. Once the electrons are transferred to NapA, they must reach the Mo-center following an unknown path.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109128
Primary Topic
Metalloenzymes and iron-sulfur proteins
Type
article
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article

Abstract 1534 Dissecting the Roles of Periplasmic Nitrate Reductase Structural Components and Their Impact on Molybdenum Cofactor Reactivity

Partha Basu, Mikayla C. Metzger, Madison Lisenko
Journal of Biological Chemistry
Metalloenzymes and iron-sulfur proteins
article

Abstract 1534 Dissecting the Roles of Periplasmic Nitrate Reductase Structural Components and Their Impact on Molybdenum Cofactor Reactivity

Partha Basu, Mikayla C. Metzger, Madison Lisenko
article en

Abstract

The reduction of nitrate by Campylobacter jejuni is catalyzed by a periplasmic nitrate reductase (Nap) complex. The catalytic subunit, NapA, harbors a molybdenum center where catalysis takes place. The catalysis relies on the molybdenum cofactor (Moco) that has a pterin-bound molybdenum center and a partner prosthetic group, an iron-sulfur cluster. Electrons are transferred to NapA during the reduction of nitrate by a second subunit called NapB, which contains diheme cytochrome c. Once the electrons are transferred to NapA, they must reach the Mo-center following an unknown path.

Journal of Biological ChemistryVol. 301(5)
Indiana University Indianapolis (US), Indiana University – Purdue University Indianapolis (US)
Openalex Percentile: Top 92%
Metalloenzymes and iron-sulfur proteins
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