ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2009
The tetraheme cytochrome from Shewanella oneidensis MR-1 shows thermodynamic bias for functional specificity of the hemes.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.
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20 citing papers in PubMed, 52 citations in OpenAlex.
- Deciphering the Mto electron uptake pathway ofApplied and environmental microbiology · 2026Article
- Sources of non-Arrhenius electron transport in bacterial nanowires.Physical chemistry chemical physics : PCCP · 2026Article
- Cytochrome "nanowires" are physically limited to sub-picoamp currents that suffice for cellular respiration.Frontiers in chemistry · 2025Article
- A Comparative Multi-Frequency EPR Study of Dipolar Interaction in Tetra-Heme Cytochromes.International journal of molecular sciences · 2023Article
- Correlated particle transport enables biological free energy transduction.Biophysical journal · 2023Article
- Investigation of the Molecular Mechanisms of the Eukaryotic Cytochrome-Biomolecules · 2022Article
- Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Protein-Embedded Metalloporphyrin Arrays Templated by Circularly Permuted Tobacco Mosaic Virus Coat Proteins.ACS nano · 2021Article
- Photoinduced hole hopping through tryptophans in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Crossing the Wall: Characterization of the Multiheme Cytochromes Involved in the Extracellular Electron Transfer Pathway ofMicroorganisms · 2021Article
- Promoting Extracellular Electron Transfer ofFrontiers in microbiology · 2021Article
- Direct evidence for heme-assisted solid-state electronic conduction in multi-hemeChemical science · 2018Article
- Modulation of the reactivity of multiheme cytochromes by site-directed mutagenesis: moving towards the optimization of microbial electrochemical technologies.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Paving the way for bioelectrotechnology: Integrating electrochemistry into bioreactors.Engineering in life sciences · 2017Article
- Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1.Frontiers in microbiology · 2015Article
- Functional characterization of the FoxE iron oxidoreductase from the photoferrotroph Rhodobacter ferrooxidans SW2.The Journal of biological chemistry · 2012Article
- Pivotal role of the strictly conserved aromatic residue F15 in the cytochrome c7 family.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Recent advances in bacterial heme protein biochemistry.Current opinion in chemical biology · 2011Review
- Thermodynamic characterization of a triheme cytochrome family from Geobacter sulfurreducens reveals mechanistic and functional diversity.Biophysical journal · 2010Article
- Molecular basis for directional electron transfer.The Journal of biological chemistry · 2010Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria of the genus Shewanella contain an abundant small tetraheme cytochrome in their periplasm when growing anaerobically. Data collected for the protein isolated from S. oneidensis MR-1 and S. frigidimarina indicate differences in the order of oxidation of the hemes. A detailed thermodynamic characterization of the cytochrome from S. oneidensis MR-1 in the physiological pH range was performed, with data collected in the pH range 5.5-9.0 from NMR experiments using partially oxidized samples and from redox titrations followed by visible spectroscopy. These data allow the parsing of the redox and redox-protonation interactions that occur during the titration of hemes. The results show that electrostatic effects dominate the heme-heme interactions, in agreement with modest redox-linked structural modifications, and protonation has a considerable influence on the redox properties of the hemes in the physiological pH range. Theoretical calculations using the oxidized and reduced structures of this protein reveal that the bulk redox-Bohr effect arises from the aggregate fractional titration of several of the heme propionates. This detailed characterization of the thermodynamic properties of the cytochrome shows that only a few of the multiple microscopic redox states that the protein can access are significantly populated at physiological pH. On this basis a functional pathway for the redox activity of the small tetraheme cytochrome from S. oneidensis MR-1 is proposed, where reduction and protonation are thermodynamically coupled in the physiological range. The differences between the small tetraheme cytochromes from the two organisms are discussed in the context of their biological role.
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