Diversity and evolution of nitric oxide reduction in bacteria and archaea
Open Access
- 20 June 2024
- journal article
- research article
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 121 (26)
Abstract
Nitrous oxide is a potent greenhouse gas whose production is catalyzed by nitric oxide reductase (NOR) members of the heme-copper oxidoreductase (HCO) enzyme superfamily. We identified several previously uncharacterized HCO families, four of which (eNOR, sNOR, gNOR, and nNOR) appear to perform NO reduction. These families have novel active-site structures and several have conserved proton channels, suggesting that they might be able to couple NO reduction to energy conservation. We isolated and biochemically characterized a member of the eNOR family from the bacterium Rhodothermus marinus and found that it performs NO reduction. These recently identified NORs exhibited broad phylogenetic and environmental distributions, greatly expanding the diversity of microbes in nature capable of NO reduction. Phylogenetic analyses further demonstrated that NORs evolved multiple times independently from oxygen reductases, supporting the view that complete denitrification evolved after aerobic respiration.Keywords
All Related Versions
Funding Information
- National Institute of Health (U12AB123456)
- Joint Genome Institute (503546)
- Joint Genome Institute (DE-AC02-05CH11231)
- DOE | SC | PNNL | Environmental Molecular Sciences Laboratory (DE-AC05-76RL01830)
This publication has 65 references indexed in Scilit:
- The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductasesJBIC Journal of Biological Inorganic Chemistry, 2016
- Aerobic denitrification: A review of important advances of the last 30 yearsBiotechnology and Bioprocess Engineering, 2015
- The cytochrome bd respiratory oxygen reductasesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2011
- Looking for the minimum common denominator in haem–copper oxygen reductases: Towards a unified catalytic mechanismBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2008
- Ligand preference and orientation in b‐ and c‐type heme‐binding proteinsProteins: Structure, Function, and Bioinformatics, 2008
- Diversity of the Heme–Copper Superfamily in Archaea: Insights from Genomics and Structural Modeling2008
- Evolution was Chemically ConstrainedJournal of Theoretical Biology, 2003
- Nitric oxide reduction, the last step in denitrification by Fusarium oxysporum, is obligatorily mediated by cytochrome P450norMolecular Genetics and Genomics, 2000
- Purification and properties of a ‘cytochrome a1’-like hemoprotein from a magnetotactic bacterium, Aquaspirillum magnetotacticumBiochimica et Biophysica Acta (BBA) - General Subjects, 1993
- Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectraAnalytical Biochemistry, 1987