CHAPTER 16

Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins

Pierre Moenne-Loccoz, Erik T. Yukl, Hirotoshi Matsumura

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Nitric oxide (NO) plays important roles as a signaling molecule and antimicrobial agent throughout biology. As with O2, many of its physiological effects are mediated by its interactions with hemoproteins. This chapter focuses on bacterial hemoproteins that function as NO sensors and NO scavengers. These functions are particularly important to pathogenic organisms as they provide a means to resist the NO produced by the host immune response. We begin by presenting structural data for NO sensor proteins that highlight mechanisms of signal transduction upon binding of NO to the heme iron. We then describe two mechanisms of NO detoxification, the NO dioxygenase and NO reductase reactions. The former is catalyzed by members of the globin family and produces nitrate (NO3 -), while the latter is catalyzed by heme/nonheme diiron NO reductases and produces nitrous oxide (N2O). A wealth of spectroscopic and rapid kinetics data on these proteins and synthetic or bioengineered analogues has begun to identify intermediates that provide insights into these physiologically important reactions.

Original languageEnglish (US)
Title of host publicationDioxygen-dependent Heme Enzymes
EditorsMasao Ikeda-Saito, Emma Raven
PublisherRoyal Society of Chemistry
Pages351-369
Number of pages19
Edition13
DOIs
StatePublished - Jan 1 2019

Publication series

NameRSC Metallobiology
Number13
Volume2019-January
ISSN (Print)2045-547X

Fingerprint

Detoxification
Nitric Oxide
Heme
Signal transduction
Globins
Sensors
Nitrous Oxide
Anti-Infective Agents
Nitrates
Signal Transduction
Proteins
Iron
Molecules
Kinetics

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology (miscellaneous)

Cite this

Moenne-Loccoz, P., Yukl, E. T., & Matsumura, H. (2019). CHAPTER 16: Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins. In M. Ikeda-Saito, & E. Raven (Eds.), Dioxygen-dependent Heme Enzymes (13 ed., pp. 351-369). (RSC Metallobiology; Vol. 2019-January, No. 13). Royal Society of Chemistry. https://doi.org/10.1039/9781788012911-00351

CHAPTER 16 : Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins. / Moenne-Loccoz, Pierre; Yukl, Erik T.; Matsumura, Hirotoshi.

Dioxygen-dependent Heme Enzymes. ed. / Masao Ikeda-Saito; Emma Raven. 13. ed. Royal Society of Chemistry, 2019. p. 351-369 (RSC Metallobiology; Vol. 2019-January, No. 13).

Research output: Chapter in Book/Report/Conference proceedingChapter

Moenne-Loccoz, P, Yukl, ET & Matsumura, H 2019, CHAPTER 16: Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins. in M Ikeda-Saito & E Raven (eds), Dioxygen-dependent Heme Enzymes. 13 edn, RSC Metallobiology, no. 13, vol. 2019-January, Royal Society of Chemistry, pp. 351-369. https://doi.org/10.1039/9781788012911-00351
Moenne-Loccoz P, Yukl ET, Matsumura H. CHAPTER 16: Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins. In Ikeda-Saito M, Raven E, editors, Dioxygen-dependent Heme Enzymes. 13 ed. Royal Society of Chemistry. 2019. p. 351-369. (RSC Metallobiology; 13). https://doi.org/10.1039/9781788012911-00351
Moenne-Loccoz, Pierre ; Yukl, Erik T. ; Matsumura, Hirotoshi. / CHAPTER 16 : Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins. Dioxygen-dependent Heme Enzymes. editor / Masao Ikeda-Saito ; Emma Raven. 13. ed. Royal Society of Chemistry, 2019. pp. 351-369 (RSC Metallobiology; 13).
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