How is NO bound to reduced copper nitrite reductase? A DFT study

Mahesh Sundararajan; Rajeev Surendran; Ian H. Hillier

doi:10.1016/j.cplett.2005.10.087

How is NO bound to reduced copper nitrite reductase? A DFT study

Mahesh Sundararajan, Rajeev Surendran, Ian H. Hillier

Research output: Contribution to journal › Article › peer-review

Abstract

Density functional theory calculations which include the enzyme environment show that NO can bind to the copper atom of reduced nitrite reductase in both side-on and end-on conformations with the end-on motif being somewhat preferred. The calculations do not predict the unusually long N-O distance found experimentally by Tocheva et al. [E.I. Tocheva, F.I. Rosell, A.G. Mauk, M.E.P. Murphy, Science 304 (2004) 867], but are in closer agreement with the structures of Antonyuk et al. [S.V. Antonyuk, R.W. Strange, G. Sawers, R.R. Eady, S.S. Hasnain, Proc. Natl. Acad. Sci. USA 102 (2005) 12041]. © 2005 Elsevier B.V. All rights reserved.

Original language	English
Pages (from-to)	96-99
Number of pages	3
Journal	Chemical Physics Letters
Volume	418
Issue number	1-3
DOIs	https://doi.org/10.1016/j.cplett.2005.10.087
Publication status	Published - 25 Jan 2006

Access to Document

10.1016/j.cplett.2005.10.087

Cite this

@article{d6b37a971d174bbcbdf9a1710da58931,

title = "How is NO bound to reduced copper nitrite reductase? A DFT study",

abstract = "Density functional theory calculations which include the enzyme environment show that NO can bind to the copper atom of reduced nitrite reductase in both side-on and end-on conformations with the end-on motif being somewhat preferred. The calculations do not predict the unusually long N-O distance found experimentally by Tocheva et al. [E.I. Tocheva, F.I. Rosell, A.G. Mauk, M.E.P. Murphy, Science 304 (2004) 867], but are in closer agreement with the structures of Antonyuk et al. [S.V. Antonyuk, R.W. Strange, G. Sawers, R.R. Eady, S.S. Hasnain, Proc. Natl. Acad. Sci. USA 102 (2005) 12041]. {\textcopyright} 2005 Elsevier B.V. All rights reserved.",

author = "Mahesh Sundararajan and Rajeev Surendran and Hillier, {Ian H.}",

year = "2006",

month = jan,

day = "25",

doi = "10.1016/j.cplett.2005.10.087",

language = "English",

volume = "418",

pages = "96--99",

journal = "Chemical Physics Letters",

issn = "1873-4448",

publisher = "Elsevier BV",

number = "1-3",

}

TY - JOUR

T1 - How is NO bound to reduced copper nitrite reductase? A DFT study

AU - Sundararajan, Mahesh

AU - Surendran, Rajeev

AU - Hillier, Ian H.

PY - 2006/1/25

Y1 - 2006/1/25

N2 - Density functional theory calculations which include the enzyme environment show that NO can bind to the copper atom of reduced nitrite reductase in both side-on and end-on conformations with the end-on motif being somewhat preferred. The calculations do not predict the unusually long N-O distance found experimentally by Tocheva et al. [E.I. Tocheva, F.I. Rosell, A.G. Mauk, M.E.P. Murphy, Science 304 (2004) 867], but are in closer agreement with the structures of Antonyuk et al. [S.V. Antonyuk, R.W. Strange, G. Sawers, R.R. Eady, S.S. Hasnain, Proc. Natl. Acad. Sci. USA 102 (2005) 12041]. © 2005 Elsevier B.V. All rights reserved.

AB - Density functional theory calculations which include the enzyme environment show that NO can bind to the copper atom of reduced nitrite reductase in both side-on and end-on conformations with the end-on motif being somewhat preferred. The calculations do not predict the unusually long N-O distance found experimentally by Tocheva et al. [E.I. Tocheva, F.I. Rosell, A.G. Mauk, M.E.P. Murphy, Science 304 (2004) 867], but are in closer agreement with the structures of Antonyuk et al. [S.V. Antonyuk, R.W. Strange, G. Sawers, R.R. Eady, S.S. Hasnain, Proc. Natl. Acad. Sci. USA 102 (2005) 12041]. © 2005 Elsevier B.V. All rights reserved.

U2 - 10.1016/j.cplett.2005.10.087

DO - 10.1016/j.cplett.2005.10.087

M3 - Article

SN - 1873-4448

VL - 418

SP - 96

EP - 99

JO - Chemical Physics Letters

JF - Chemical Physics Letters

IS - 1-3

ER -

How is NO bound to reduced copper nitrite reductase? A DFT study

Abstract

Access to Document

Fingerprint

Cite this