Identification of a tyrosine switch in copper-haem nitrite reductases

IUCrJ
Jianshu DongS Samar Hasnain

Abstract

There are few cases where tyrosine has been shown to be involved in catalysis or the control of catalysis despite its ability to carry out chemistry at much higher potentials (1 V versus NHE). Here, it is shown that a tyrosine that blocks the hydrophobic substrate-entry channel in copper-haem nitrite reductases can be activated like a switch by the treatment of crystals of Ralstonia pickettii nitrite reductase (RpNiR) with nitric oxide (NO) (-0.8 ± 0.2 V). Treatment with NO results in an opening of the channel originating from the rotation of Tyr323 away from AspCAT97. Remarkably, the structure of a catalytic copper-deficient enzyme also shows Tyr323 in the closed position despite the absence of type 2 copper (T2Cu), clearly demonstrating that the status of Tyr323 is not controlled by T2Cu or its redox chemistry. It is also shown that the activation by NO is not through binding to haem. It is proposed that activation of the Tyr323 switch is controlled by NO through proton abstraction from tyrosine and the formation of HNO. The insight gained here for the use of tyrosine as a switch in catalysis has wider implications for catalysis in biology.

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Citations

Nov 21, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Kakali SenThomas W Keal
Nov 25, 2020·The Journal of Physical Chemistry. B·Bryan KudischGregory D Scholes
Jun 8, 2021·Chemical Science·Michael A HoughS Samar Hasnain

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Methods Mentioned

BETA
electron paramagnetic resonance

Software Mentioned

MOSFLM
MOLE
AIMLESS
REFMAC
CCP
MolProbity
XDS
PyMOL

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