ArticleNature2015
The octahaem MccA is a haem c-copper sulfite reductase.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Multiheme selenoenzyme essential for elemental sulfur respiration.Science advances · 2026Article
- Demonstration of the Role of Both a Ttr and a Psr Homologue Enzymes in the Respiration of Tetrathionate by an Environmental Bacterium Shewanella sp. ANA-3.Environmental microbiology · 2026Article
- A survey of the Desulfuromonadia "cytochromome" provides a glimpse of the unexplored diversity of multiheme cytochromes in nature.BMC genomics · 2024Article
- Article
- Microbial functionalities and immobilization of environmental lead: Biogeochemical and molecular mechanisms and implications for bioremediation.Journal of hazardous materials · 2023Review
- Article
- Structures of the CcmABCD heme release complex at multiple states.Nature communications · 2022Article
- A New Paradigm of Multiheme Cytochrome Evolution by Grafting and Pruning Protein Modules.Molecular biology and evolution · 2022Article
- Microbial communities of Auka hydrothermal sediments shed light on vent biogeography and the evolutionary history of thermophily.The ISME journal · 2022Article
- Architecture of the membrane-bound cytochrome c heme lyase CcmF.Nature chemical biology · 2021Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Phylogenomic analysis of novel Diaforarchaea is consistent with sulfite but not sulfate reduction in volcanic environments on early Earth.The ISME journal · 2020Article
- Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Article
- Regulation of Respiratory Pathways in Campylobacterota: A Review.Frontiers in microbiology · 2019Review
- Expanded diversity of microbial groups that shape the dissimilatory sulfur cycle.The ISME journal · 2018Article
- The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The six-electron reduction of sulfite to sulfide is the pivot point of the biogeochemical cycle of the element sulfur. The octahaem cytochrome c MccA (also known as SirA) catalyses this reaction for dissimilatory sulfite utilization by various bacteria. It is distinct from known sulfite reductases because it has a substantially higher catalytic activity and a relatively low reactivity towards nitrite. The mechanistic reasons for the increased efficiency of MccA remain to be elucidated. Here we show that anoxically purified MccA exhibited a 2- to 5.5-fold higher specific sulfite reductase activity than the enzyme isolated under oxic conditions. We determined the three-dimensional structure of MccA to 2.2 Å resolution by single-wavelength anomalous dispersion. We find a homotrimer with an unprecedented fold and haem arrangement, as well as a haem bound to a CX15CH motif. The heterobimetallic active-site haem 2 has a Cu(I) ion juxtaposed to a haem c at a Fe-Cu distance of 4.4 Å. While the combination of metals is reminiscent of respiratory haem-copper oxidases, the oxidation-labile Cu(I) centre of MccA did not seem to undergo a redox transition during catalysis. Intact MccA tightly bound SO2 at haem 2, a dehydration product of the substrate sulfite that was partially turned over due to photoreduction by X-ray irradiation, yielding the reaction intermediate SO. Our data show the biometal copper in a new context and function and provide a chemical rationale for the comparatively high catalytic activity of MccA.
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