The high-molecular-weight cytochrome c Cyc2 of Acidithiobacillus ferrooxidans is an outer membrane protein.
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Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidansMariprofundus ferrooxydans PV-1 the first genome of a marine Fe(II) oxidizing ZetaproteobacteriumCharacteristics and adaptability of iron- and sulfur-oxidizing microorganisms used for the recovery of metals from minerals and their concentratesThe pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1.Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans: a high throughput proteomics analysis.Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications.The gill chamber epibiosis of deep-sea shrimp Rimicaris exoculata: an in-depth metagenomic investigation and discovery of Zetaproteobacteria.New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph.Terminal oxidase diversity and function in "Metallosphaera yellowstonensis": gene expression and protein modeling suggest mechanisms of Fe(II) oxidation in the sulfolobales.Characterization of an OmpA-like outer membrane protein of the acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidansMetabolic diversity among main microorganisms inside an arsenic-rich ecosystem revealed by meta- and proteo-genomicsMetaproteomic evidence of changes in protein expression following a change in electrode potential in a robust biocathode microbiome.Identification and Characterization of MtoA: A Decaheme c-Type Cytochrome of the Neutrophilic Fe(II)-Oxidizing Bacterium Sideroxydans lithotrophicus ES-1.In situ Spectroscopy on Intact Leptospirillum ferrooxidans Reveals that Reduced Cytochrome 579 is an Obligatory Intermediate in the Aerobic Iron Respiratory Chain.Characterization of cytochrome 579, an unusual cytochrome isolated from an iron-oxidizing microbial communityExtracellular respiration.Identification of components of electron transport chains in the extremely thermoacidophilic crenarchaeon Metallosphaera sedula through iron and sulfur compound oxidation transcriptomesDifferential protein expression during growth of Acidithiobacillus ferrooxidans on ferrous iron, sulfur compounds, or metal sulfides.Are gram-positive bacteria capable of electron transfer across their cell wall without an externally available electron shuttle?Metatranscriptomic evidence of pervasive and diverse chemolithoautotrophy relevant to C, S, N and Fe cycling in a shallow alluvial aquifer.Mineral respiration under extreme acidic conditions: from a supramolecular organization to a molecular adaptation in Acidithiobacillus ferrooxidans.The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant.Characterization of the petI and res operons of Acidithiobacillus ferrooxidans.The fox operon from Rhodobacter strain SW2 promotes phototrophic Fe(II) oxidation in Rhodobacter capsulatus SB1003.From chemolithoautotrophs to electrolithoautotrophs: CO2 fixation by Fe(II)-oxidizing bacteria coupled with direct uptake of electrons from solid electron sources.Comparative Genomic Analysis of Neutrophilic Iron(II) Oxidizer Genomes for Candidate Genes in Extracellular Electron Transfer.Proteomic Analysis of Differential Protein Expression in Acidithiobacillus ferrooxidans Grown on Ferrous Iron or Elemental SulfurMetatranscriptomics Supports the Mechanism for Biocathode Electroautotrophy by "Candidatus Tenderia electrophaga".Type IV pili of Acidithiobacillus ferrooxidans can transfer electrons from extracellular electron donors.Effect of metal sulfide pulp density on gene expression of electron transporters in Acidithiobacillus sp. FJ2.Increases of ferrous iron oxidation activity and arsenic stressed cell growth by overexpression of Cyc2 in Acidithiobacillus ferrooxidans ATCC19859.Multi-heme cytochromes provide a pathway for survival in energy-limited environments.Cytochrome 572 is a conspicuous membrane protein with iron oxidation activity purified directly from a natural acidophilic microbial community.Increase in Fe2+-producing activity during growth of Acidithiobacillus ferrooxidans ATCC23270 on sulfur.Adaptive responses of chemolithoautotrophic acidophilic Acidithiobacillus ferrooxidans to sewage sludge.Respiratory isozyme, two types of rusticyanin of Acidithiobacillus ferrooxidans.Ferrous iron oxidation by sulfur-oxidizing Acidithiobacillus ferrooxidans and analysis of the process at the levels of transcription and protein synthesis.Metaproteogenomic Profiling of Microbial Communities Colonizing Actively Venting Hydrothermal Chimneys.The Confluence of Heavy Metal Biooxidation and Heavy Metal Resistance: Implications for Bioleaching by Extreme ThermoacidophilesStructural Analysis of Respirasomes in Electron Transfer Pathway of Acidithiobacillus ferrooxidans: A Computer-Aided Molecular Designing Study
P2860
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P2860
The high-molecular-weight cytochrome c Cyc2 of Acidithiobacillus ferrooxidans is an outer membrane protein.
description
2002 nî lūn-bûn
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2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The high-molecular-weight cyto ...... s is an outer membrane protein
@nl
The high-molecular-weight cyto ...... is an outer membrane protein.
@ast
The high-molecular-weight cyto ...... is an outer membrane protein.
@en
type
label
The high-molecular-weight cyto ...... s is an outer membrane protein
@nl
The high-molecular-weight cyto ...... is an outer membrane protein.
@ast
The high-molecular-weight cyto ...... is an outer membrane protein.
@en
prefLabel
The high-molecular-weight cyto ...... s is an outer membrane protein
@nl
The high-molecular-weight cyto ...... is an outer membrane protein.
@ast
The high-molecular-weight cyto ...... is an outer membrane protein.
@en
P2093
P2860
P1476
The high-molecular-weight cyto ...... is an outer membrane protein.
@en
P2093
Andrés Yarzábal
Danielle Lemesle-Meunier
Gaël Brasseur
Jeanine Ratouchniak
John A DeMoss
Karen Lund
Violaine Bonnefoy
P2860
P304
P356
10.1128/JB.184.1.313-317.2002
P407
P577
2002-01-01T00:00:00Z