ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2010
A systematic investigation of multiheme c-type cytochromes in prokaryotes.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 81 citations in OpenAlex.
- Ghost-rocks' microbiota: metagenomic insights into their influence on the biogeochemistry of karstic cave and groundwater.FEMS microbiology ecology · 2026Article
- A survey of the Desulfuromonadia "cytochromome" provides a glimpse of the unexplored diversity of multiheme cytochromes in nature.BMC genomics · 2024Article
- A Comparative Multi-Frequency EPR Study of Dipolar Interaction in Tetra-Heme Cytochromes.International journal of molecular sciences · 2023Article
- A New Paradigm of Multiheme Cytochrome Evolution by Grafting and Pruning Protein Modules.Molecular biology and evolution · 2022Article
- Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Homogeneous Cytochrome 579 Is an Octamer That Reacts Too Slowly With Soluble Iron to Be the Initial Iron Oxidase in the Respiratory Chain ofFrontiers in microbiology · 2021Article
- Article
- Role of multiheme cytochromes involved in extracellular anaerobic respiration in bacteria.Protein science : a publication of the Protein Society · 2020Review
- Diverse Microorganisms in Sediment and Groundwater Are Implicated in Extracellular Redox Processes Based on Genomic Analysis of Bioanode Communities.Frontiers in microbiology · 2020Article
- Novel Extracellular Electron Transfer Channels in a Gram-Positive Thermophilic Bacterium.Frontiers in microbiology · 2020Article
- Improvement of sabinene tolerance ofBiotechnology for biofuels · 2020Article
- Properties and structure of a low-potential, penta-heme cytochrome cPhotosynthesis research · 2019Article
- Capability for arsenic mobilization in groundwater is distributed across broad phylogenetic lineages.PloS one · 2019Article
- Genomic Insights Into Energy Metabolism ofFrontiers in microbiology · 2018Article
- Comparative Genomic Analysis of Neutrophilic Iron(II) Oxidizer Genomes for Candidate Genes in Extracellular Electron Transfer.Frontiers in microbiology · 2017Article
- Minimal Functional Sites in Metalloproteins and Their Usage in Structural Bioinformatics.International journal of molecular sciences · 2016Review
- Stable and Variable Parts of Microbial Community in Siberian Deep Subsurface Thermal Aquifer System Revealed in a Long-Term Monitoring Study.Frontiers in microbiology · 2016Article
- Comparative Proteomic Analysis of Desulfotomaculum reducens MI-1: Insights into the Metabolic Versatility of a Gram-Positive Sulfate- and Metal-Reducing Bacterium.Frontiers in microbiology · 2016Article
- Molecular dissection of a putative iron reductase from Desulfotomaculum reducens MI-1.Biochemical and biophysical research communications · 2015Article
- Identification of proteins capable of metal reduction from the proteome of the Gram-positive bacterium Desulfotomaculum reducens MI-1 using an NADH-based activity assay.Environmental microbiology · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multiheme c-type cytochromes (MHCs) are metalloproteins that can play various biochemical roles, including enzymatic activity and electron transfer. As electron transfer proteins, the presence of multiple heme cofactors in the vicinity allows electrons to rapidly travel relatively long distances. MHCs are often characterized by relatively low structural complexity, with the heme cofactors being largely responsible for maintaining the structure in place, owing to the protein-heme covalent linkages. In this work, we analyzed an extensive ensemble of 594 complete prokaryotic proteomes, amounting to more than 1.9 million sequences, to characterize their content in MHCs. We identified 1,659 MHCs in 258 organisms. The presence of MHCs was found to correlate quite well with the capability of an organism to synthesize or take up heme. For two organisms, the presence of MHCs in the proteome could be taken as a hint to the presence of divergent heme uptake pathways. The most common numbers of heme-binding motifs in a sequence were four (25%) and two (23%), followed by five (13%) and ten (9.8%). The average protein-to-heme ratio was relatively similar for all MHCs, except diheme proteins, regardless of the number of motifs at around 60 +/- 30. The latter ratio could in favorable cases be a useful indicator for functional assignments of novel MHCs. Finally, we showed that the amount of structural information currently available for MHCs is limited with respect to the diversity of this broad class of metalloproteins. Experimental efforts in the structural investigation of MHCs are thus warranted.
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