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The structure of the diheme cytochrome c4 from Neisseria gonorrhoeae reveals multiple contributors to tuning reduction potentials

Journal of Inorganic Biochemistry(2024)10.1016/j.jinorgbio.2024.112496Source: DataRank Database

The structure of the diheme cytochrome c4 from Neisseria gonorrhoeae reveals multiple contributors to tuning reduction potentials is a research paper published in Journal of Inorganic Biochemistry (2024). On theSindex it has a DataRank of 0. It has been cited 1 time.

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Enrichment:Funding (12 grants)Impact (FWCI 0.16)OA: greenTopics (40)IDs (PubMed, PMC, OpenAlex)Annotations (2)SDGs (1)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (4)

Morgan E. Reik,Michael J. Ragusa ORCID,Ekaterina V. Pletneva ORCID,Fangfang Zhong ORCID

Live enrichment

PubMed:38330683 PMC:PMC11034767 OpenAlex:https://openalex.org/W4391179585

National Institute of General Medical Sciences

Grant: P30GM133893

Biological and Environmental Research

Grant: KP1607011

Brookhaven National Laboratory

Grant: DE-SC0012704

U.S. Department of Energy

Grant: DE-SC0024330

National Institutes of Health

Grant: 17-ID-1

National Institutes of Health

Grant: P20-GM113132

National Institutes of Health

Grant: R01-GM098502

National Institutes of Health

Grant: R35 GM128663

National Institutes of Health

Grant: T32 AI007519

NIGMS NIH HHS

Grant: P20 GM113132

NIGMS NIH HHS

Grant: R01 GM098502

Office of Science

FWCI

0.16

Citation Percentile

0.5%

Citation Trend

2025

greenLicense: http://www.elsevier.com/open-access/userlicense/1.0/

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC11034767/pdf/nihms-1981242.pdf

publisherhttps://api.elsevier.com/content/article/PII:S0162013424000199?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0162013424000199?httpAccept=text/plain

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/11034767

Fields of Study

Porphyrin Metabolism and DisordersHemoglobin structure and functionPhotosynthetic Processes and MechanismsHumansNeisseria gonorrhoeaeOxidation-ReductionCytochromes cOxidoreductasesHemeIronSolvents

MeSH Terms

HemeHumansIronNeisseria gonorrhoeaeOxidation-ReductionOxidoreductasesSolventsCytochromes c

Keywords

HemeChemistryCytochromeHemeproteinElectron transferProtein structurePseudomonas stutzeriRedoxNeisseria gonorrhoeaeCrystallographyBiophysicsBiochemistryBacteriaPhotochemistryGeneticsBiologyEnzymeInorganic chemistryHeme ProteinsReduction PotentialsInterdomain Interface

Sustainable Development Goals

SDG 0: Life in Land

The structure of the diheme cytochrome c4 from Neisseria gonorrhoeae reveals multiple contributors to tuning reduction potentials

FAIR Checklist

Authors (4)

Funding (12 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)