Minimal ATP‐Independent N <sub>2</sub> ‐Reducing Systems Defined by L‐Cluster‐Bound Nitrogenase Assembly Platforms

-like enzyme that preceded the modern, high-efficiency two-component system; whereas the shared L-cluster topology found in ancient nondiazotrophic enzymes like methyl-CoM reductase and methylthio-alkane reductase further implies that the L-cluster may represent an evolutionary link among nitrogen, carbon, and sulfur biogeochemical cycles.

Authors

Robert Quechol
Markus Walter Ribbe (ORCID: https://orcid.org/0000-0002-7366-1526)
Chi Chung Lee (ORCID: https://orcid.org/0000-0002-5266-6686)
Yimo Yang (ORCID: https://orcid.org/0009-0001-2117-8890)
Yilin Hu (ORCID: https://orcid.org/0000-0002-9088-2865)

Institutions

University of California, Irvine (US)

Publication Details

Journal: Angewandte Chemie International Edition
Published: 2026-04-27
DOI: https://doi.org/10.1002/anie.2968123
Primary Topic: Metalloenzymes and iron-sulfur proteins
Type: article
Field-Weighted Citation Impact: 0.00

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article

Minimal ATP‐Independent N ₂ ‐Reducing Systems Defined by L‐Cluster‐Bound Nitrogenase Assembly Platforms

Robert Quechol, Markus Walter Ribbe, Chi Chung Lee, Yimo Yang et al.

Apr 27, 2026

Angewandte Chemie International Edition

Metalloenzymes and iron-sulfur proteins

article

Minimal ATP‐Independent N ₂ ‐Reducing Systems Defined by L‐Cluster‐Bound Nitrogenase Assembly Platforms

Robert Quechol, Markus Walter Ribbe, Chi Chung Lee, Yimo Yang, Yilin Hu

April 27, 2026article en

Abstract

-like enzyme that preceded the modern, high-efficiency two-component system; whereas the shared L-cluster topology found in ancient nondiazotrophic enzymes like methyl-CoM reductase and methylthio-alkane reductase further implies that the L-cluster may represent an evolutionary link among nitrogen, carbon, and sulfur biogeochemical cycles.

Angewandte Chemie International Edition

University of California, Irvine (US)

Clean water and sanitation

Openalex Percentile: Top 17%

Metalloenzymes and iron-sulfur proteins

DOI Open Access PDF OpenAlex

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