Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity (Q44557676)

4 December 2017

title

Two aspartic acid residues in the PSST-homologous NUKM subunit of complex I from Yarrowia lipolytica are essential for catalytic activity (English)

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4 December 2017

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5

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4 December 2017

Aurelio Garofano

1

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4 December 2017

Klaus Zwicker

series ordinal

2

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4 December 2017

Stefan Kerscher

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3

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4 December 2017

Pamela Okun

series ordinal

4

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4 December 2017

language of work or name

English

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publication date

20 August 2003

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Journal of Biological Chemistry

4 December 2017

number of pages

6

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based on heuristic

inferred from page(s)

published in

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4 December 2017

volume

278

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4 December 2017

issue

43

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4 December 2017

page(s)

42435-42440

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Analysis of the subunit composition of complex I from bovine heart mitochondria

4 December 2017

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EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ

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21 January 2018

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21 January 2018

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21 January 2018

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Function of Conserved Acidic Residues in the PSST Homologue of Complex I (NADH:Ubiquinone Oxidoreductase) fromYarrowia lipolytica

21 January 2018

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21 January 2018

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Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone

21 January 2018

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Two EPR-detectable [4Fe-4S] clusters, N2a and N2b, are bound to the NuoI (TYKY) subunit of NADH:ubiquinone oxidoreductase (Complex I) from Rhodobacter capsulatus.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M305819200

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4 December 2017

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