Alternative Type II NAD(P)H Dehydrogenases in the Mitochondria of Protists and Fungi

被引:18
作者
Antos-Krzeminska, Nina [1 ]
Jarmuszkiewicz, Wieslawa [1 ]
机构
[1] Adam Mickiewicz Univ, Dept Bioenerget, Umultowska 89, PL-61614 Poznan, Poland
关键词
Protists; fungi; rotenone-insensitive NAD(P)H dehydrogenases; mitochondrial electron transport chain; energy metabolism; INSENSITIVE NADH DEHYDROGENASE; ELECTRON-TRANSPORT CHAIN; COMPLEX-I; PLASMODIUM-FALCIPARUM; RESPIRATORY-CHAIN; NADH/UBIQUINONE OXIDOREDUCTASE; UBIQUINONE OXIDOREDUCTASE; TOXOPLASMA-GONDII; ESCHERICHIA-COLI; POTENTIAL SOURCE;
D O I
10.1016/j.protis.2018.11.001
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Plants, fungi, and some protists possess a more branched electron transport chain in their mitochondria compared to canonical one. In these organisms, the electron transport chain contains several rotenone-insensitive NAD(P)H dehydrogenases. Some are located on the outer surface, and others are located on the inner surface of the inner mitochondrial membrane. The putative role of these enzymes still remains elusive, but they may prevent the overreduction of the electron transport chain components and decrease the production of reaction oxygen species as a consequence. The last two decades resulted in the discovery of alternative rotenone-insensitive NAD(P)H dehydrogenases present in representatives of fungi and protozoa. The aim of this review is to gather and focus on current information concerning molecular and functional properties, regulation, and the physiological role of fungal and protozoan alternative NAD(P)H dehydrogenases. (C) 2018 The Authors. Published by Elsevier GmbH.
引用
收藏
页码:21 / 37
页数:17
相关论文
共 86 条
[1]   External NAD(P)H Dehydrogenases in Acanthamoeba castellanii Mitochondria [J].
Antos-Krzeminska, Nina ;
Jarmuszkiewicz, Wieslawa .
PROTIST, 2014, 165 (05) :580-593
[2]   Functional expression of the Acanthamoeba castellanii alternative oxidase in Escherichia coli; regulation of the activity and evidence for Acaox gene function [J].
Antos-Krzeminska, Nina ;
Jarmuszkiewicz, Wieslawa .
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE, 2014, 92 (03) :235-241
[3]   OXIDATION OF REDUCED NICOTINAMIDE ADENINE-DINUCLEOTIDE PHOSPHATE BY POTATO MITOCHONDRIA - INHIBITION BY SULFHYDRYL-REAGENTS [J].
ARRON, GP ;
EDWARDS, GE .
PLANT PHYSIOLOGY, 1980, 65 (04) :591-594
[4]   The respiratory chain of the thermophilic archaeon Sulfolobus metallicus:: studies on the type-II NADH dehydrogenase [J].
Bandeiras, TM ;
Salgueiroa, CA ;
Huber, H ;
Gomes, CM ;
Teixeira, M .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2003, 1557 (1-3) :13-19
[5]   Acidianus ambivalens type-II NADH dehydrogenase:: genetic characterisation and identification of the flavin moiety as FMN [J].
Bandeiras, TM ;
Salgueiro, C ;
Kletzin, A ;
Gomes, CM ;
Teixeira, M .
FEBS LETTERS, 2002, 531 (02) :273-277
[6]   Functional characterization and target validation of alternative complex I of Plasmodium falciparum mitochondria [J].
Biagini, GA ;
Viriyavejakul, P ;
O'Neill, PM ;
Bray, PG ;
Ward, SA .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2006, 50 (05) :1841-1851
[7]   MITOCHONDRIAL DEVELOPMENT IN TRYPANOSOMA-BRUCEI-BRUCEI TRANSITIONAL BLOOD-STREAM FORMS [J].
BIENEN, EJ ;
SARIC, M ;
POLLAKIS, G ;
GRADY, RW ;
CLARKSON, AB .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1991, 45 (02) :185-192
[8]   Purification of the 45 kDa, membrane bound NADH dehydrogenase of Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone analogues [J].
Björklöf, K ;
Zickermann, V ;
Finel, M .
FEBS LETTERS, 2000, 467 (01) :105-110
[9]   Cryptosporidium Pathogenicity and Virulence [J].
Bouzid, Maha ;
Hunter, Paul R. ;
Chalmers, Rachel M. ;
Tyler, Kevin M. .
CLINICAL MICROBIOLOGY REVIEWS, 2013, 26 (01) :115-134
[10]   The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria [J].
Carneiro, P ;
Duarte, M ;
Videira, A .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2004, 1608 (01) :45-52