Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties.
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The chemistry and biochemistry of heme c: functional bases for covalent attachmentAutocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A familyModification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex.In vitro formation of a c-type cytochrome.Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.A heme-based redox sensor in the methanogenic archaeon Methanosarcina acetivoransOrder within a mosaic distribution of mitochondrial c-type cytochrome biogenesis systems?Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersProbing why trypanosomes assemble atypical cytochrome c with an AxxCH haem-binding motif instead of CxxCH.Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.Variation of the axial haem ligands and haem-binding motif as a probe of the Escherichia coli c-type cytochrome maturation (Ccm) system.Maturation of the unusual single-cysteine (XXXCH) mitochondrial c-type cytochromes found in trypanosomatids must occur through a novel biogenesis pathway.The Escherichia coli cytochrome c maturation (Ccm) system does not detectably attach heme to single cysteine variants of an apocytochrome c.Interaction of heme with variants of the heme chaperone CcmE carrying active site mutations and a cleavable N-terminal His tag.Stereoselective in vitro formation of c-type cytochrome variants from Hydrogenobacter thermophilus containing only a single thioether bond.In vitro studies on thioether bond formation between Hydrogenobacter thermophilus apocytochrome c(552) with metalloprotoporphyrin derivatives.Covalent bonding of heme to protein prevents heme capture by nontypeable Haemophilus influenzae.The magnetosome proteins MamX, MamZ and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense.Biosynthesis of Single Thioether c-Type Cytochromes Provides Insight into Mechanisms Intrinsic to Holocytochrome c Synthase (HCCS).
P2860
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P2860
Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties.
description
2000 nî lūn-bûn
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2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
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2000年论文
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name
Loss of either of the two heme ...... on physicochemical properties.
@en
type
label
Loss of either of the two heme ...... on physicochemical properties.
@en
prefLabel
Loss of either of the two heme ...... on physicochemical properties.
@en
P2860
P356
P1476
Loss of either of the two heme ...... on physicochemical properties.
@en
P2093
Ferguson SJ
Tomlinson EJ
P2860
P304
32530-32534
P356
10.1074/JBC.M004022200
P407
P577
2000-10-01T00:00:00Z