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Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina.

Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK
Biochemistry 41 8551-6 (2002)
Cited: 8 times
EuropePMC logo PMID: 12093271

Abstract

The X-ray structure of the soluble fumarate reductase from Shewanella frigidimarina [Taylor, P., Pealing, S. L., Reid, G. A., Chapman, S. K., and Walkinshaw, M. D. (1999) Nat. Struct. Biol. 6, 1108-1112] clearly shows the presence of an internally bound sodium ion. This sodium ion is coordinated by one solvent water molecule (Wat912) and five backbone carbonyl oxygens from Thr506, Met507, Gly508, Glu534, and Thr536 in what is best described as octahedral geometry (despite the rather long distance from the sodium ion to the backbone oxygen of Met507 (3.1 A)). The water ligand (Wat912) is, in turn, hydrogen bonded to the imidazole ring of His505. This histidine residue is adjacent to His504, a key active-site residue thought to be responsible for the observed pK(a) of the enzyme. Thus, it is possible that His505 may be important in both maintaining the sodium site and in influencing the active site. Here we describe the crystallographic and kinetic characterization of the H505A and H505Y mutant forms of the Shewanella fumarate reductase. The crystal structures of both mutant forms of the enzyme have been solved to 1.8 and 2.0 A resolution, respectively. Both show the presence of the sodium ion in the equivalent position to that found in the wild-type enzyme. The structure of the H505A mutant shows the presence of two water molecules in place of the His505 side-chain which form part of a hydrogen-bonding network with Wat48, a ligand to the sodium ion. The structure of the H505Y mutant shows the hydroxyl group of the tyrosine side-chain hydrogen-bonding to a water molecule which is also a ligand to the sodium ion. Apart from these features, there are no significant structural alterations as a result of either substitution. Both the mutant enzymes are catalytically active but show markedly different pH profiles compared to the wild-type enzyme. At high pH (above 8.5), the wild type and mutant enzymes have very similar activities. However, at low pH (6.0), the H505A mutant enzyme is some 20-fold less active than wild-type. The combined crystallographic and kinetic results suggest that His505 is not essential for sodium binding but does affect catalytic activity perhaps by influencing the pK(a) of the adjacent His504.

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  1. Imidazole and nitroimidazole derivatives as NADH-fumarate reductase inhibitors: Density functional theory studies, homology modeling, and molecular docking. Campos-Fernández L, Ortiz-Muñiz R, Cortés-Barberena E, Mares-Sámano S, Garduño-Juárez R, Soriano-Correa C. J Comput Chem 43 1573-1595 (2022)


Reviews citing this publication (4)

  1. Function and structure of complex II of the respiratory chain. Cecchini G. Annu Rev Biochem 72 77-109 (2003)
  2. Catalytic mechanisms of complex II enzymes: a structural perspective. Iverson TM. Biochim Biophys Acta 1827 648-657 (2013)
  3. Metabolic adaptation of Pseudomonas pseudoalcaligenes CECT5344 to cyanide: role of malate-quinone oxidoreductases, aconitase and fumarase isoenzymes. Igeño MI, Becerra G, Guijo MI, Merchán F, Blasco R. Biochem Soc Trans 39 1849-1853 (2011)
  4. An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond. Iverson TM, Singh PK, Cecchini G. J Biol Chem 299 104761 (2023)

Articles citing this publication (3)

  1. A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II. Tomasiak TM, Maklashina E, Cecchini G, Iverson TM. J Biol Chem 283 15460-15468 (2008)
  2. Identification and characterization of a novel fumarase gene by metagenome expression cloning from marine microorganisms. Jiang C, Wu LL, Zhao GC, Shen PH, Jin K, Hao ZY, Li SX, Ma GF, Luo FF, Hu GQ, Kang WL, Qin XM, Bi YL, Tang XL, Wu B. Microb Cell Fact 9 91 (2010)
  3. Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR. Pessanha M, Rothery EL, Louro RO, Turner DL, Miles CS, Reid GA, Chapman SK, Xavier AV, Salgueiro CA. FEBS Lett 578 185-190 (2004)


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