LSTM Home > LSTM Research > LSTM Online Archive

Chapter 17 Type II NADH: Quinone Oxidoreductases of Plasmodium Falciparum and Mycobacterium Tuberculosis. Kinetic and High-Throughput Assays

Fisher, Nicholas, Warman, Ashley, Ward, Stephen ORCID: https://orcid.org/0000-0003-2331-3192 and Biagini, Giancarlo ORCID: https://orcid.org/0000-0001-6356-6595 (2010) 'Chapter 17 Type II NADH: Quinone Oxidoreductases of Plasmodium Falciparum and Mycobacterium Tuberculosis. Kinetic and High-Throughput Assays' in: Allison, W. S. and Scheffler, I. E., (eds) Methods in Enzymology, 456, San Diego, Calif., Academic Press, pp. 303-320.

Full text not available from this repository.

Abstract

Type II NADH: quinone oxidoreductases (ndh) are flavoenzymes found in a broad range of organisms including plants, fungi, protozoa, and bacteria. The ndh enzymes catalyze the oxidation of NADH with concomitant reduction of quinone (Q). These membrane-bound respiratory enzymes differ from the canonical NADH: dehydrogenase (complex I), because they are not involved in the vectorial transfer of protons across membranes. In Plasmodium falciparum and Mycobacterium tuberculosis, causative agents of malaria and tuberculosis, respectively, ndhs have aroused interest because of the essential role played in maintaining a reduced Q-pool during infection. In this chapter, we present methods for the measurement of steady-state parameters for ndhs from both pathogens, highlighting best practices and caveats. In addition, owing to the interest in ndhs as potential chemotherapeutic targets, we describe a miniaturized endpoint assay that is validated for high-throughput screening (HTS) of chemical libraries. © 2009 Elsevier Inc. All rights reserved.

Item Type: Book Section
Additional Information: doi: 10.1016/S0076-6879(08)04417-0 PubMed ID: 19348896 Correspondence Address: Fisher, N.; Liverpool School of Tropical Medicine, Pembroke Place, Liverpool, United Kingdom Chemicals/CAS: reduced nicotinamide adenine dinucleotide, 58-68-4; NADH dehydrogenase (quinone), 1.6.99.5; Quinone Reductases, 1.6.99.-
Uncontrolled Keywords: recombinant protein reduced nicotinamide adenine dinucleotide clinical practice enzyme metabolism Escherichia coli heterologous expression Mycobacterium tuberculosis nonhuman Plasmodium falciparum priority journal protein function protein structure respiratory chain review steady state Animals Kinetics Quinone Reductases Fungi Protozoa
Subjects: QX Parasitology > Protozoa > QX 135 Plasmodia
Faculty: Department: Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group
Digital Object Identifer (DOI): https://doi.org/10.1016/S0076-6879(08)04417-0
Depositing User: Mary Creegan
Date Deposited: 17 Nov 2010 12:19
Last Modified: 06 Feb 2018 12:59
URI: http://archive.lstmed.ac.uk/id/eprint/267

Statistics

View details

Actions (login required)

Edit Item Edit Item