ArticleBiochemistry2007
Heme attachment motif mobility tunes cytochrome c redox potential.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- A Divergent Mitochondrial Cytochrome c in Malaria Parasites With an Anomalously Low Redox Potential.Journal of molecular biology · 2026Article
- Structural basis of Neisseria meningitidis quinol dependent nitric oxide reductase activation by dimerization.Communications biology · 2026Article
- A Divergent CytochromebioRxiv : the preprint server for biology · 2025Article
- The flexible chain: regulation of structure and activity of ETC complexes defines rate of ATP synthesis and sites of superoxide generation.Biophysical reviews · 2025Review
- Secondary Sphere Lewis Acid Activated Heme Superoxo Adducts Mimic Crucial Non-Covalent Interactions in IDO/TDO Heme Dioxygenases.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Combined spectroscopic and structural approaches to explore the mechanism of histidine-ligated heme-dependent aromatic oxygenases.Methods in enzymology · 2023Article
- Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case.Molecules (Basel, Switzerland) · 2022Review
- Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Human CytochromeBiochemistry · 2020Article
- Quantitative Photo-crosslinking Mass Spectrometry Revealing Protein Structure Response to Environmental Changes.Analytical chemistry · 2019Article
- Redesign of a Copper Storage Protein into an Artificial Hydrogenase.ACS catalysis · 2019Article
- pH-Induced Switch between Different Modes of CytochromeACS omega · 2019Article
- Influence of heme c attachment on heme conformation and potential.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.Journal of biomolecular NMR · 2015Article
- Effects of protein structure on iron-polypeptide vibrational dynamic coupling in cytochrome c.Biochemistry · 2015Article
- Article
- Article
- The influence of heme ruffling on spin densities in ferricytochromes c probed by heme core 13C NMR.Inorganic chemistry · 2013Article
- Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure.Chembiochem : a European journal of chemical biology · 2013Article
- Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Hydrogen exchange (HX) rates and midpoint potentials (Em) of variants of cytochrome c from Pseudomonas aeruginosa (Pa cyt c551) and Hydrogenobacter thermophilus (Ht cyt c552) have been characterized in an effort to develop an understanding of the impact of properties of the Cys-X-X-Cys-His pentapeptide c-heme attachment (CXXCH) motif on heme redox potential. Despite structural conservation of the CXXCH motif, Ht cyt c552 exhibits a low level of protection from HX for amide protons within this motif relative to Pa cyt c551. Site-directed mutants have been prepared to determine the structural basis for and functional implications of these variations on HX behavior. The double mutant Ht-M13V/K22M displays suppressed HX within the CXXCH motif as well as a decreased Em (by 81 mV), whereas the corresponding double mutant of Pa cyt c551 (V13M/M22K) exhibits enhanced HX within the CXXCH pentapeptide and a modest increase in Em (by 30 mV). The changes in Em correlate with changes in axial His chemical shifts in the ferric proteins reflecting the extent of histidinate character. Thus, the mobility of the CXXCH pentapeptide is found to impact the His-Fe(III) interaction and therefore the heme redox potential.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.