Interaction of Terminal Oxidases with Amphipathic Molecules

被引：2

作者：

Azarkina, Natalia V. V. ^{[1
]}

Borisov, Vitaliy B. B. ^{[1
]}

Oleynikov, Ilya P. P. ^{[1
]}

Sudakov, Roman V. V. ^{[1
]}

Vygodina, Tatiana V. V. ^{[1
]}

机构：

[1] Lomonosov Moscow State Univ, Belozersky Inst Physicochem Biol, Leninskie Gory 1,Bld 40, Moscow 119992, Russia

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2023年 / 24卷 / 07期

基金：

俄罗斯科学基金会;

关键词：

molecular bioenergetics; terminal oxidases; cytochrome oxidase; bile acid-binding site; amphipathic ligands; tight bound lipids; detergents; regulation; CYTOCHROME-C-OXIDASE; ELECTRON-TRANSFER; PROTON-TRANSFER; PARACOCCUS-DENITRIFICANS; RHODOBACTER-SPHAEROIDES; BOUND CARDIOLIPIN; BINDING SITES; BA(3) OXIDASE; NITRIC-OXIDE; ACTIVE-SITE;

D O I：

10.3390/ijms24076428

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The review focuses on recent advances regarding the effects of natural and artificial amphipathic compounds on terminal oxidases. Terminal oxidases are fascinating biomolecular devices which couple the oxidation of respiratory substrates with generation of a proton motive force used by the cell for ATP production and other needs. The role of endogenous lipids in the enzyme structure and function is highlighted. The main regularities of the interaction between the most popular detergents and terminal oxidases of various types are described. A hypothesis about the physiological regulation of mitochondrial-type enzymes by lipid-soluble ligands is considered.

引用

页数：17

共 103 条

[1] A role for the protein in internal electron transfer to the catalytic center of cytochrome C oxidase [J].

Antalik, M ;

Jancura, D ;

Palmer, G ;

Fabian, M .

BIOCHEMISTRY, 2005, 44 (45) :14881-14889

[2] Cardiolipin binding in bacterial respiratory complexes: Structural and functional implications [J].

Arias-Cartin, Rodrigo ;

Grimaldi, Stephane ;

Arnoux, Pascal ;

Guigliarelli, Bruno ;

Magalon, Axel .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2012, 1817 (10) :1937-1949

[3] Cardiolipin-based respiratory complex activation in bacteria [J].

Arias-Cartin, Rodrigo ;

Grimaldi, Stephane ;

Pommier, Janine ;

Lanciano, Pascal ;

Schaefer, Cedric ;

Arnoux, Pascal ;

Giordano, Gerard ;

Guigliarelli, Bruno ;

Magalon, Axel .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (19) :7781-7786

[4] Identification of cardiolipin binding sites on cytochrome c oxidase at the entrance of proton channels [J].

Arnarez, C. ;

Marrink, S. J. ;

Periole, X. .

SCIENTIFIC REPORTS, 2013, 3

[5] 3,5-diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP [J].

Arnold, S ;

Goglia, F ;

Kadenbach, B .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 252 (02) :325-330

[6] Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase [J].

Arnold, S ;

Kadenbach, B .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 249 (01) :350-354

[7] Cardiolipin enhances the enzymatic activity of cytochrome bd and cytochrome bo3 solubilized in dodecyl-maltoside [J].

Asseri, Amer H. ;

Godoy-Hernandez, Albert ;

Goojani, Hojjat Ghasemi ;

Lill, Holger ;

Sakamoto, Junshi ;

McMillan, Duncan G. G. ;

Bald, Dirk .

SCIENTIFIC REPORTS, 2021, 11 (01)

[8] TIGHTLY BOUND CARDIOLIPIN IN CYTOCHROME OXIDASE [J].

AWASTHI, YC ;

CHUANG, TF ;

KEENAN, TW ;

CRANE, FL .

BIOCHIMICA ET BIOPHYSICA ACTA, 1971, 226 (01) :42-&

[9] Ornithine lipid is required for optimal steady-state amounts of c-type cytochromes in Rhodobacter capsulatus [J].

Aygun-Sunar, Semra ;

Mandaci, Sevnur ;

Koch, Hans-George ;

Murray, Ian V. J. ;

Goldfine, Howard ;

Daldal, Fevzi .

MOLECULAR MICROBIOLOGY, 2006, 61 (02) :418-435

[10] Effect of Membrane Environment on the Ligand-Binding Properties of the Terminal Oxidase Cytochrome bd-I from Escherichia coli [J].

Borisov, V. B. .

BIOCHEMISTRY-MOSCOW, 2020, 85 (12-13) :1603-1612

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