Structure and mechanism of copper-carbonic anhydrase II: a nitrite reductase.

IUCrJ
Jacob T AndringRobert McKenna

Abstract

Nitric oxide (NO) promotes vasodilation through the activation of guanylate cyclase, resulting in the relaxation of the smooth muscle vasculature and a subsequent decrease in blood pressure. Therefore, its regulation is of interest for the treatment and prevention of heart disease. An example is pulmonary hypertension which is treated by targeting this NO/vasodilation pathway. In bacteria, plants and fungi, nitrite (NO2 -) is utilized as a source of NO through enzymes known as nitrite reductases. These enzymes reduce NO2 - to NO through a catalytic metal ion, often copper. Recently, several studies have shown nitrite reductase activity of mammalian carbonic anhydrase II (CAII), yet the molecular basis for this activity is unknown. Here we report the crystal structure of copper-bound human CAII (Cu-CAII) in complex with NO2 - at 1.2 Å resolution. The structure exhibits Type 1 (T-1) and 2 (T-2) copper centers, analogous to bacterial nitrite reductases, both required for catalysis. The copper-substituted CAII active site is penta-coordinated with a 'side-on' bound NO2 -, resembling a T-2 center. At the N terminus, several residues that are normally disordered form a porphyrin ring-like configuration surrounding a second copper, ac...Continue Reading

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Citations

Mar 10, 2020·IUCrJ·Anders Liljas
Sep 13, 2020·Nature Communications·Jin Kyun KimChae Un Kim
Jan 30, 2021·Journal of Enzyme Inhibition and Medicinal Chemistry·Dimitrios Tsikas, Stepan Gambaryan
Feb 23, 2021·Journal of Enzyme Inhibition and Medicinal Chemistry·Alessio NocentiniClaudiu T Supuran
Aug 11, 2020·Biochimica Et Biophysica Acta. Bioenergetics·Sasmit S Deshmukh, László Kálmán
Sep 11, 2020·Biophysical Journal·Bengt-Harald Jonsson, Anders Liljas
Jun 30, 2021·Inorganic Chemistry·Molly StaufferTimothy H Warren

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Methods Mentioned

BETA
nuclear
X-ray
NMR

Software Mentioned

CCP
Coot
AIMLESS
Phenix
LigPlot +
PyMOL

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