Biosynthesis of artificial microperoxidases by exploiting the secretion and cytochrome c maturation apparatuses of Escherichia coli
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The chemistry and biochemistry of heme c: functional bases for covalent attachmentNanostructures for peroxidasesControlled Protein Dimerization through Hybrid Coordination MotifsEvolution of Metal Selectivity in Templated Protein InterfacesIn Vitro and Cellular Self-Assembly of a Zn-Binding Protein Cryptand via Templated Disulfide BondsA designed supramolecular protein assembly with in vivo enzymatic activityMolecular Basis Behind Inability of Mitochondrial Holocytochrome c Synthase to Mature Bacterial Cytochromes: DEFINING A CRITICAL ROLE FOR CYTOCHROME c α HELIX-1.Streptococcus gordonii utilizes several distinct gene functions to recruit Porphyromonas gingivalis into a mixed community.Cytochrome c maturation and the physiological role of c-type cytochromes in Vibrio cholerae.Introduction of a covalent histidine-heme linkage in a hemoglobin: a promising tool for heme protein engineering.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.Composition and function of cytochrome c biogenesis System II.Cytochrome c biogenesis System I.Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.Linking ultrastructure and function in four genera of anaerobic ammonium-oxidizing bacteria: cell plan, glycogen storage, and localization of cytochrome C proteins.The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatusComparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis.Modular and versatile hybrid coordination motifs on alpha-helical protein surfacesCytochrome c heme lyase can mature a fusion peptide composed of the amino-terminal residues of horse cytochrome c.Structure and Catalysis of Fe(III) and Cu(II) Microperoxidase-11 Interacting with the Positively Charged Interfaces of Lipids.Totally synthetic microperoxidase-11.Insights into the relationship between the haem-binding pocket and the redox potential ofc6cytochromes: four atomic resolution structures ofc6andc6-like proteins fromSynechococcussp. PCC 7002
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P2860
Biosynthesis of artificial microperoxidases by exploiting the secretion and cytochrome c maturation apparatuses of Escherichia coli
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 24 August 2004
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Biosynthesis of artificial mic ...... pparatuses of Escherichia coli
@en
Biosynthesis of artificial mic ...... paratuses of Escherichia coli.
@nl
type
label
Biosynthesis of artificial mic ...... pparatuses of Escherichia coli
@en
Biosynthesis of artificial mic ...... paratuses of Escherichia coli.
@nl
prefLabel
Biosynthesis of artificial mic ...... pparatuses of Escherichia coli
@en
Biosynthesis of artificial mic ...... paratuses of Escherichia coli.
@nl
P2860
P356
P1476
Biosynthesis of artificial mic ...... pparatuses of Escherichia coli
@en
P2093
Linda Thöny-Meyer
Martin Braun
P2860
P304
12830-12835
P356
10.1073/PNAS.0402435101
P407
P577
2004-08-24T00:00:00Z