The Crystal Structure of Heme D1 Biosynthesis-Associated Small C-Type Cytochrome NirC Reveals Mixed Oligomeric States in Crystallo

doi 10.1101/2020.02.21.959056

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February 21, 2020

Authors

Thomas Klünemann

Steffi Henke

Wulf Blankenfeldt

Publisher

Cold Spring Harbor Laboratory

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The Crystal Structure of Heme D1 Biosynthesis-Associated Small C-Type Cytochrome NirC Reveals Mixed Oligomeric States in Crystallo

Full Text

Abstract

Date

Authors

Publisher

Related search

Interaction of HoloCcmE With CcmF in Heme Trafficking and Cytochrome C Biosynthesis

The Crystal Structure of the Extracellular 11-Heme Cytochrome UndA Reveals a Conserved 10-Heme Motif and Defined Binding Site for Soluble Iron Chelates

Crystal Structure of Chloroplast Cytochrome Freveals a Novel Cytochrome Fold and Unexpected Heme Ligation

Conversion of a C Type Cytochrome to a B Type That Spontaneously Forms in Vitro From Apo Protein and Heme: Implications for C Type Cytochrome Biogenesis and Folding

Crystal Structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction During Vancomycin Biosynthesis

The Crystal Structure of the Cytochrome P450 Enzyme TxtE

Crystal Structure of StnA for the Biosynthesis of Antitumor Drug Streptonigrin Reveals a Unique Substrate Binding Mode

3P107 X-Ray Structural Analysis of the Bovine Heart Cytochrome C Oxidase in the Mixed Valence State(Hemeproteins. Electronic States. Proteins-Structure and Structure-Function Relationship,Oral Presentations)

Crystal Structure of the Dimeric C-Terminal Domain of TonB Reveals a Novel Fold