Loss of Complex I activity in the Escherichia coli enzyme results from truncating the C-terminus of subunit K, but not from cross-linking it to subunits N or L
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Loss of Complex I activity in the Escherichia coli enzyme results from truncating the C-terminus of subunit K, but not from cross-linking it to subunits N or L
Authors
Keywords
Complex I, Cross-linking, Subunit interactions, Methanethiosulfonate, nuoK
Journal
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
Volume 48, Issue 3, Pages 325-333
Publisher
Springer Nature
Online
2016-03-01
DOI
10.1007/s10863-016-9655-y
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation
- (2015) Shaotong Zhu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I
- (2015) Stefan Steimle et al. MOLECULAR MICROBIOLOGY
- Architecture of mammalian respiratory complex I
- (2014) Kutti R. Vinothkumar et al. NATURE
- Mitochondrial Complex I
- (2013) Judy Hirst Annual Review of Biochemistry
- Structure and function of the C-terminal domain of MrpA in theBacillus subtilisMrp-antiporter complex - The evolutionary progenitor of the long horizontal helix in complex I
- (2013) Egle Virzintiene et al. FEBS LETTERS
- Energy Transducing Roles of Antiporter-like Subunits inEscherichia coliNDH-1 with Main Focus on Subunit NuoN (ND2)
- (2013) Motoaki Sato et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Crystal structure of the entire respiratory complex I
- (2013) Rozbeh Baradaran et al. NATURE
- Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I
- (2012) Stefan Steimle et al. FEBS LETTERS
- Energy-converting respiratory Complex I: On the way to the molecular mechanism of the proton pump
- (2012) Marina Verkhovskaya et al. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
- Roles of Subunit NuoK (ND4L) in the Energy-transducing Mechanism ofEscherichia coliNDH-1 (NADH:Quinone Oxidoreductase)
- (2012) Jesus Torres-Bacete et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Role of Subunit NuoL for Proton Translocation by Respiratory Complex I
- (2011) Stefan Steimle et al. BIOCHEMISTRY
- Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli
- (2011) Heiko Erhardt et al. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
- Structural Contribution of C-terminal Segments of NuoL (ND5) and NuoM (ND4) Subunits of Complex I fromEscherichia coli
- (2011) Jesus Torres-Bacete et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Probing the mechanistic role of the long α-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis
- (2011) Galina Belevich et al. MOLECULAR MICROBIOLOGY
- Structure of the membrane domain of respiratory complex I
- (2011) Rouslan G. Efremov et al. NATURE
- Mutagenesis of the L, M, and N Subunits of Complex I from Escherichia coli Indicates a Common Role in Function
- (2011) Jose Michel et al. PLoS One
- The Membrane Subunit NuoL(ND5) Is Involved in the Indirect Proton Pumping Mechanism ofEscherichia coliComplex I
- (2010) Eiko Nakamaru-Ogiso et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Features of Subunit NuoM (ND4) in Escherichia coli NDH-1
- (2009) Jesus Torres-Bacete et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I)
- (2008) Liliya Euro et al. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Add your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started