In vitro formation of a c-type cytochrome. - Wikidata - wikimedia - TriplyDB

In vitro formation of a c-type cytochrome.

In vitro formation of a c-type cytochrome.

http://www.wikidata.org/entity/Q34030217

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Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp The chemistry and biochemistry of heme c: functional bases for covalent attachment Cytochrome c maturation system on the negative side of bioenergetic membranes: CCB or System IV A strategic protein in cytochrome c maturation: three-dimensional structure of CcmH and binding to apocytochrome c Cytochrome c as an experimental model protein.Molecular modeling of cytochrome b₅ with a single cytochrome c-like thioether linkage.Tuning the formation of a covalent haem-protein link by selection of reductive or oxidative conditions as exemplified by ascorbate peroxidase.Going wireless: Fe(III) oxide reduction without pili by Geobacter sulfurreducens strain JS-1.The CcmE protein of the c-type cytochrome biogenesis system: unusual in vitro heme incorporation into apo-CcmE and transfer from holo-CcmE to apocytochrome.The acidic nature of the CcmG redox-active center is important for cytochrome c maturation in Escherichia coli.Introduction of a covalent histidine-heme linkage in a hemoglobin: a promising tool for heme protein engineering.C-type cytochromes: diverse structures and biogenesis systems pose evolutionary problems.Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination.During Cytochrome c Maturation CcmI Chaperones the Class I Apocytochromes until the Formation of Their b-Type Cytochrome Intermediates Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins Biliprotein maturation: the chromophore attachment.The heme chaperone ApoCcmE forms a ternary complex with CcmI and apocytochrome c Continued surprises in the cytochrome c biogenesis story.A heme-based redox sensor in the methanogenic archaeon Methanosarcina acetivorans Covalent heme attachment to the protein in human heme oxygenase-1 with selenocysteine replacing the His25 proximal iron ligand.Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control.Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette.Cytochrome c biogenesis: the Ccm system.Cytochrome c biogenesis in mitochondria--Systems III and V.Cytochrome c biogenesis System I.The active-site cysteinyls and hydrophobic cavity residues of ResA are important for cytochrome c maturation in Bacillus subtilis Geometric constraints for porphyrin binding in helical protein binding sites.A pivotal heme-transfer reaction intermediate in cytochrome c biogenesis.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.High stability of apo-cytochrome c' from thermophilic Hydrogenophilus thermoluteolus.Effects of heme on the thermal stability of mesophilic and thermophilic cytochromes c: comparison between experimental and theoretical results.Compensatory thio-redox interactions between DsbA, CcdA and CcmG unveil the apocytochrome c holdase role of CcmG during cytochrome c maturation.The Escherichia coli cytochrome c maturation (Ccm) system does not detectably attach heme to single cysteine variants of an apocytochrome c.Cytochrome c maturation. The in vitro reactions of horse heart apocytochrome c and Paracoccus dentrificans apocytochrome c550 with heme.Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis.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.A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system.NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.

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P2860

In vitro formation of a c-type cytochrome.

http://www.wikidata.org/entity/Q34030217

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2002 nî lūn-bûn

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

In vitro formation of a c-type cytochrome.

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In vitro formation of a c-type cytochrome.

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In vitro formation of a c-type cytochrome.

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type

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In vitro formation of a c-type cytochrome.

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In vitro formation of a c-type cytochrome.

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In vitro formation of a c-type cytochrome.

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In vitro formation of a c-type cytochrome.

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In vitro formation of a c-type cytochrome.

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In vitro formation of a c-type cytochrome.

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

P1476

In vitro formation of a c-type cytochrome.

@en

P2093

Anthony C Willis

http://www.w3.org/2001/XMLSchema#string

James W A Allen

http://www.w3.org/2001/XMLSchema#string

Oliver Daltrop

http://www.w3.org/2001/XMLSchema#string

Stuart J Ferguson

http://www.w3.org/2001/XMLSchema#string

P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Structure of cytochrome c nitrite reductase

Solution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogeneous binding of the heme

The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea

Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy

Mitochondrial coproporphyrinogen oxidase and protoporphyrin formation

Reassessment of Ellman's reagent

CytochromecFolding and Unfolding: A Biphasic Mechanism

Still a puzzle: why is haem covalently attached in c-type cytochromes?

Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c

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7872-7876

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10.1073/PNAS.132259099

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12

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99

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2002-06-01T00:00:00Z

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