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Structural Insight into Evolution of the Quinone Binding Site in Complex II

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Abstract

The Complex II family encompasses membrane bound succinate:quinones reductases and quinol:fumarate reductases that catalyze interconversion of succinate and fumarate coupled with reduction and oxidation of quinone. These enzymes are found in all biological genres and share a modular structure where a highly conserved soluble domain is bound to a membrane-spanning domain that is represented by distinct variations. The current classification of the complex II family members is based on the number of subunits and co-factors in the membrane anchor (types A-F). This classification also provides insights into possible evolutionary paths and suggests that some of the complex II enzymes (types A-C) co-evolved as the whole assembly. Origin of complex II types D and F may have arisen from independent events of de novo association of the conserved soluble domain with a new anchor. Here we analyze a recent structure of Mycobacterium smegmatis Sdh2, a complex II enzyme with two transmembrane subunits and two heme b molecules. This analysis supports an earlier hypothesis suggesting that mitochondrial complex II (type C) with a single heme b may have evolved as an assembled unit from an ancestor similar to M. smegmatis Sdh2.

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Abbreviations

CII:

complex II

cryo-EM:

cryo-electron microscopy

heme b D :

distal heme b

heme b P :

proximal heme b

QFR:

quinol:fumarate oxidoreductase

QD :

distal quinone binding site

QP :

proximal quinone binding site

SQR:

succinate:quinone reductase

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Acknowledgments

I dedicate this review to my mentor Andrei Vinogradov. He devoted a large portion of his scientific life to study mitochondrial complex II, which he often called “my first love in science”. I also wish to thank Gary Cecchini for reading the manuscript.

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  1. Department of Biochemistry and Biophysics, University of California, San Francisco, 94143, San Francisco, CA, USA

    Elena Maklashina

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Correspondence to Elena Maklashina.

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The author declares no conflicts of interest. This article does not contain description of studies with the involvement of humans or animal subjects.

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Maklashina, E. Structural Insight into Evolution of the Quinone Binding Site in Complex II. Biochemistry Moscow 87, 752–761 (2022). https://doi.org/10.1134/S0006297922080077

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