Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways
about
Development of recombinant hemoglobin-based oxygen carriersCytochrome c as an experimental model protein.CcsBA is a cytochrome c synthetase that also functions in heme transportHeme ligand identification and redox properties of the cytochrome c synthetase, CcmFMitochondrial cytochrome c biogenesis: no longer an enigma.Control of DegP-dependent degradation of c-type cytochromes by heme and the cytochrome c maturation system in Escherichia coli.The CcmC:heme:CcmE complex in heme trafficking and cytochrome c biosynthesisHuman mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome cTopology and function of CcmD in cytochrome c maturationRegulation of intracellular heme trafficking revealed by subcellular reportersA conserved haem redox and trafficking pathway for cofactor attachment.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.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.Metal-substituted protein MRI contrast agents engineered for enhanced relaxivity and ligand sensitivity.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 genomics sheds light on niche differentiation and the evolutionary history of comammox Nitrospira.Metal and redox selectivity of protoporphyrin binding to the heme chaperone CcmE.
P2860
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P2860
Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Heme concentration dependence ...... cytochrome c assembly pathways
@en
Heme concentration dependence ...... cytochrome c assembly pathways
@nl
type
label
Heme concentration dependence ...... cytochrome c assembly pathways
@en
Heme concentration dependence ...... cytochrome c assembly pathways
@nl
prefLabel
Heme concentration dependence ...... cytochrome c assembly pathways
@en
Heme concentration dependence ...... cytochrome c assembly pathways
@nl
P2093
P2860
P356
P1476
Heme concentration dependence ...... cytochrome c assembly pathways
@en
P2093
Cynthia L Richard-Fogal
Elaine R Frawley
Robert E Feissner
Robert G Kranz
P2860
P304
P356
10.1128/JB.01388-06
P577
2006-11-03T00:00:00Z