CcsBA is a cytochrome c synthetase that also functions in heme transport - Wikidata - awgldk - TriplyDB

CcsBA is a cytochrome c synthetase that also functions in heme transport

CcsBA is a cytochrome c synthetase that also functions in heme transport

http://www.wikidata.org/entity/Q30488404

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Kinetics and specificity of feline leukemia virus subgroup C receptor (FLVCR) export function and its dependence on hemopexin Cytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pylori Conserved residues of the human mitochondrial holocytochrome c synthase mediate interactions with heme Mechanisms of mitochondrial holocytochrome c synthase and the key roles played by cysteines and histidine of the heme attachment site, Cys-XX-Cys-His Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds.Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Topologically conserved residues direct heme transport in HRG-1-related proteins.Unique flexibility in energy metabolism allows mycobacteria to combat starvation and hypoxia.The 2-Cys peroxiredoxin alkyl hydroperoxide reductase c binds heme and participates in its intracellular availability in Streptococcus agalactiae.CCS5, a thioredoxin-like protein involved in the assembly of plastid c-type cytochromes Cytochrome c assembly.Control of intracellular heme levels: heme transporters and heme oxygenases Characterization of DsbD in Neisseria meningitidis.Identification of the type II cytochrome c maturation pathway in anammox bacteria by comparative genomics.Complete genome sequence of the fish pathogen Flavobacterium branchiophilum Heme ligand identification and redox properties of the cytochrome c synthetase, CcmF Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor.Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231.Mitochondrial cytochrome c biogenesis: no longer an enigma.New PCR primers targeting hydrazine synthase and cytochrome c biogenesis proteins in anammox bacteria.The CcmC:heme:CcmE complex in heme trafficking and cytochrome c biosynthesis Human mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome c Heme and FLVCR-related transporter families SLC48 and SLC49.His protects heme as it crosses the membrane A conserved haem redox and trafficking pathway for cofactor attachment.Trafficking of heme and porphyrins in metazoa.Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control.Interaction of holoCcmE with CcmF in heme trafficking and cytochrome c biosynthesis.The CcmFH complex is the system I holocytochrome c synthetase: engineering cytochrome c maturation independent of CcmABCDE.Composition and function of cytochrome c biogenesis System II.Physiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling.Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins.Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.Maturation of Plastid c-type Cytochromes.Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability.CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid Cytochrome c Assembly in the Green Alga Chlamydomonas reinhardtii.Essential histidine pairs indicate conserved haem binding in epsilonproteobacterial cytochrome c haem lyases.Substrate specificity of three cytochrome c haem lyase isoenzymes from Wolinella succinogenes: unconventional haem c binding motifs are not sufficient for haem c attachment by NrfI and CcsA1.Comparative Analyses of Transport Proteins Encoded within the Genomes of Bdellovibrio bacteriovorus HD100 and Bdellovibrio exovorus JSS.

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P2860

CcsBA is a cytochrome c synthetase that also functions in heme transport

http://www.wikidata.org/entity/Q30488404

description

2009 nî lūn-bûn

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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

@zh-tw

2009年论文

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name

CcsBA is a cytochrome c synthetase that also functions in heme transport

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CcsBA is a cytochrome c synthetase that also functions in heme transport

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type

label

CcsBA is a cytochrome c synthetase that also functions in heme transport

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CcsBA is a cytochrome c synthetase that also functions in heme transport

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prefLabel

CcsBA is a cytochrome c synthetase that also functions in heme transport

@ast

CcsBA is a cytochrome c synthetase that also functions in heme transport

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PNAS.0903132106

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Proceedings of the National Academy of Sciences of the United States of America

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CcsBA is a cytochrome c synthetase that also functions in heme transport

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P2093

Elaine R Frawley

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Robert G Kranz

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P2860

Identification of a human heme exporter that is essential for erythropoiesis

Identification of a mammalian mitochondrial porphyrin transporter

Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly

Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins

ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis

Identification of an intestinal heme transporter

Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels

The nrfI gene is essential for the attachment of the active site haem group of Wolinella succinogenes cytochrome c nitrite reductase.

Ccs1, a nuclear gene required for the post-translational assembly of chloroplast c-type cytochromes.

The distinct heme coordination environments and heme-binding stabilities of His39Ser and His39Cys mutants of cytochrome b5.

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10201-10206

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scholarly article

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10.1073/PNAS.0903132106

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25

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106

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2009-06-09T00:00:00Z

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