Get Advances in bacterial pathogen biology PDF

By Robert K. Poole

ISBN-10: 0128001429

ISBN-13: 9780128001424

ISBN-10: 0128003057

ISBN-13: 9780128003053

This quantity is an up to date evaluate of the body structure of chosen pathogenic micro organism. each one bankruptcy is written via specialists within the box of that organism.The concentration is on biochemistry and body structure yet subject matters of medical relevance are included.

Key features:

  • Contributions from prime experts
  • Informs and updates on all of the most modern advancements within the box

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Extra info for Advances in bacterial pathogen biology

Example text

There is also evidence that the complex is essential in the Gram-negative H. pylori (McGowan, Cover, & Blaser, 1997). This may reflect the cellular ATP demands of this strictly respiratory pathogen. , 1996). , 1997; Tran & Cook, 2005). This is an intriguing observation given the universal distribution of this enzyme in bacterial cells and its central role in cellular ATP homeostasis. This may reflect the ability of ATP generation by substratelevel phosphorylation to sustain the growth of most bacterial cells on fermentable carbon sources, where increased glycolytic flux can compensate for the 38 Gregory M.

Jacobs W. , Cook, G. M. (2014). An obligately aerobic soil bacterium activates fermentative hydrogen production to survive reductive stress during hypoxia. Proceedings of the National Academy of Sciences of the United States of America, 111, 11479–11484. Bertsova, Y. , & Bogachev, A. V. (2004). The origin of the sodium-dependent NADH oxidation by the respiratory chain of Klebsiella pneumoniae. FEBS Letters, 563, 207–212. Betts, J. , Lukey, P. , Robb, L. , McAdam, R. , & Duncan, K. (2002). Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling.

Thomer, A. (1993). On the mechanism of sodium ion translocation by oxaloacetate decarboxylase of Klebsiella pneumoniae. Biochemistry, 32, 1734–1739. , & Poole, R. K. (1995). The oxygen affinity of cytochrome bo’ in Escherichia coli determined by the deoxygenation of oxyleghemoglobin and oxymyoglobin: Km values for oxygen are in the submicromolar range. Journal of Bacteriology, 177, 867–870. , & Poole, R. K. (1996). The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: Implications for regulation of activity in vivo by oxygen inhibition.

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Advances in bacterial pathogen biology by Robert K. Poole


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