The University of Southampton
University of Southampton Institutional Repository

Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins. A chemical discussion of the differential biological effects of these redox related products of NOS

Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins. A chemical discussion of the differential biological effects of these redox related products of NOS
Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins. A chemical discussion of the differential biological effects of these redox related products of NOS
Investigations on the biological effects of nitric oxide (NO) derived from nitric oxide synthase (NOS) have led to an explosion in biomedical research over the last decade. The chemistry of this diatomic radical is key to its biological effects. Recently, nitroxyl (HNO/NO(-)) has been proposed to be another important constituent of NO biology. However, these redox siblings often exhibit orthogonal behavior in physiological and cellular responses. We therefore explored the chemistry of NO and HNO with heme proteins in different redox states and observed that HNO favors reaction with ferric heme while NO favors ferrous, consistent with previous reports. Further results show that HNO and NO were equally effective in inhibiting cytochrome P450 activity, which involves ferric and ferrous complexes. The differential chemical behavior of NO and HNO toward heme proteins provides insight into mechanisms of activity that not only helps explain some of the opposing effects observed in NOS-mediated events, but offers a unique control mechanism for the biological action of NO.
nitric oxide, nitroxyl, angeli’s salt, heme, horseradish peroxidase, myoglobin, hemoglobin
0162-0134
52-60
Miranda, Katrina M.
128fa814-eb00-472f-a5e7-5657e59ac9b9
Nims, Raymond W.
61b5e338-729f-4729-b80b-ed184a632122
Thomas, Douglas D.
b685f80a-b4f5-42fa-b90f-3b7ec1ed6b7a
Espey, Michael G.
ee9fa59b-ebe3-46cd-a86c-cd1659f99331
Citrin, Deborah
c8e6cf3e-3337-4f9f-aeae-4686e76846c9
Bartberger, Michael D.
c8b30326-b3cc-4af8-9987-fa512ff7692e
Paolocci, Nazareno
d674c5c7-7f14-462d-bda9-1ee8a4ab5b8a
Fukuto, Jon M.
222058bd-beef-4b4e-856c-54b1fc7eb4a9
Feelisch, Martin
8c1b9965-8614-4e85-b2c6-458a2e17eafd
Wink, David A.
008b5aec-8c2b-4035-8912-fb6fd530413c
Miranda, Katrina M.
128fa814-eb00-472f-a5e7-5657e59ac9b9
Nims, Raymond W.
61b5e338-729f-4729-b80b-ed184a632122
Thomas, Douglas D.
b685f80a-b4f5-42fa-b90f-3b7ec1ed6b7a
Espey, Michael G.
ee9fa59b-ebe3-46cd-a86c-cd1659f99331
Citrin, Deborah
c8e6cf3e-3337-4f9f-aeae-4686e76846c9
Bartberger, Michael D.
c8b30326-b3cc-4af8-9987-fa512ff7692e
Paolocci, Nazareno
d674c5c7-7f14-462d-bda9-1ee8a4ab5b8a
Fukuto, Jon M.
222058bd-beef-4b4e-856c-54b1fc7eb4a9
Feelisch, Martin
8c1b9965-8614-4e85-b2c6-458a2e17eafd
Wink, David A.
008b5aec-8c2b-4035-8912-fb6fd530413c

Miranda, Katrina M., Nims, Raymond W., Thomas, Douglas D., Espey, Michael G., Citrin, Deborah, Bartberger, Michael D., Paolocci, Nazareno, Fukuto, Jon M., Feelisch, Martin and Wink, David A. (2003) Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins. A chemical discussion of the differential biological effects of these redox related products of NOS. Journal of Inorganic Biochemistry, 93 (1-2), 52-60. (doi:10.1016/S0162-0134(02)00498-1). (PMID:12538052)

Record type: Article

Abstract

Investigations on the biological effects of nitric oxide (NO) derived from nitric oxide synthase (NOS) have led to an explosion in biomedical research over the last decade. The chemistry of this diatomic radical is key to its biological effects. Recently, nitroxyl (HNO/NO(-)) has been proposed to be another important constituent of NO biology. However, these redox siblings often exhibit orthogonal behavior in physiological and cellular responses. We therefore explored the chemistry of NO and HNO with heme proteins in different redox states and observed that HNO favors reaction with ferric heme while NO favors ferrous, consistent with previous reports. Further results show that HNO and NO were equally effective in inhibiting cytochrome P450 activity, which involves ferric and ferrous complexes. The differential chemical behavior of NO and HNO toward heme proteins provides insight into mechanisms of activity that not only helps explain some of the opposing effects observed in NOS-mediated events, but offers a unique control mechanism for the biological action of NO.

This record has no associated files available for download.

More information

Published date: 1 January 2003
Keywords: nitric oxide, nitroxyl, angeli’s salt, heme, horseradish peroxidase, myoglobin, hemoglobin
Organisations: Clinical & Experimental Sciences

Identifiers

Local EPrints ID: 337858
URI: http://eprints.soton.ac.uk/id/eprint/337858
ISSN: 0162-0134
PURE UUID: 93d60dd5-6208-4cc6-bc7c-adea4061e3b2
ORCID for Martin Feelisch: ORCID iD orcid.org/0000-0003-2320-1158

Catalogue record

Date deposited: 22 Jun 2012 10:48
Last modified: 15 Mar 2024 03:41

Export record

Altmetrics

Contributors

Author: Katrina M. Miranda
Author: Raymond W. Nims
Author: Douglas D. Thomas
Author: Michael G. Espey
Author: Deborah Citrin
Author: Michael D. Bartberger
Author: Nazareno Paolocci
Author: Jon M. Fukuto
Author: Martin Feelisch ORCID iD
Author: David A. Wink

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×