The Globins of Campylobacter jejuni - Advances in Microbial Physiology - page 142

Sellars, M. J., Hall, S. J., & Kelly, D. J. (2002). Growth of Campylobacter jejuni supported by
respiration of fumarate, nitrate, nitrite, trimethylamine-N-oxide, or dimethyl sulfoxide
requires oxygen. Journal of Bacteriology , 184 , 4187-4196.
Shepherd, M., Barynin, V., Lu, C., Bernhardt, P. V., Wu, G., Yeh, S. R., et al. (2010). The
single-domain globin from the pathogenic bacterium Campylobacter jejuni : Novel D-helix
conformation, proximal hydrogen bonding that influences ligand binding, and
peroxidase-like redox properties. The Journal of Biological Chemistry , 285 , 12747-12754.
Shepherd, M., Bernhardt, P. V., & Poole, R. K. (2011). Globin-mediated nitric oxide detox-
ification in the foodborne pathogenic bacterium Campylobacter jejuni proceeds via a
dioxygenase or denitrosylase mechanism. Nitric Oxide , 25 , 229-233.
Sies, H. (1991). Oxidative stress II. Oxidants and antioxidants. London: Academic Press.
Simonsen, J., Teunis, P., van Pelt, W., van Duynhoven, Y., Krogfelt, K. A., Sadkowska-
Todys, M., et al. (2011). Usefulness of seroconversion rates for comparing infection pres-
sures between countries. Epidemiology and Infection , 139 , 636-643.
Singh, R. J., Hogg, N., Joseph, J., & Kalyanaraman, B. (1996). Mechanism of nitric oxide
release from S -nitrosothiols. The Journal of Biological Chemistry , 271 , 18596-18603.
Skirrow, M. B. (2006). John McFadyean and the centenary of the first isolation of Campylo-
bacter species. Clinical Infectious Diseases , 43 , 1213-1217.
Smith, M. A., Finel, M., Korolik, V., & Mendz, G. L. (2000). Characteristics of the aerobic
respiratory chains of the microaerophiles Campylobacter jejuni and Helicobacter pylori .
Archives of Microbiology , 174 , 1-10.
Smith, A., Hill, S., & Anthony, C. (1990). The purification, characterization and role of the
d -type cytochrome oxidase of Klebsiella pneumoniae during nitrogen fixation. Journal of
General Microbiology , 136 , 171-180.
Smith, H. K., Shepherd, M., Monk, C., Green, J., & Poole, R. K. (2011). The
NO-responsive hemoglobins of Campylobacter jejuni : Concerted responses of two globins
to NO and evidence in vitro for globin regulation by the transcription factor NssR. Nitric
Oxide , 25 , 234-241.
Spiro, T. G., & Wasbotten, I. H. (2005). CO as a vibrational probe of heme protein active
sites. Journal of Inorganic Biochemistry , 99 , 34-44.
Stevanin, T. M., Ioannidis, N., Mills, C. E., Kim, S. O., Hughes, M. N., & Poole, R. K.
(2000). Flavohemoglobin Hmp affords inducible protection for Escherichia coli respira-
tion, catalyzed by cytochromes bo' or bd , from nitric oxide. The Journal of Biological Chem-
istry , 275 , 35868-35875.
Stuehr, D. J. (1999). Mammalian nitric oxide synthases. Biochimica et Biophysica Acta , 1411 ,
217-230.
Suschek, C. V., Schewe, T., Sies, H., & Kroncke, K. D. (2006). Nitrite, a naturally occurring
precursor of nitric oxide that acts like a 'prodrug'. Biological Chemistry , 387 , 499-506.
Svensson, L., Poljakovic, M., Save, S., Gilberthorpe, N., Schon, T., Strid, S., et al. (2010).
Role of flavohemoglobin in combating nitrosative stress in uropathogenic Escherichia
coli—Implications for urinary tract infection. Microbial Pathogenesis , 49 , 59-66.
Tam, C. C., O'Brien, S. J., Petersen, I., Islam, A., Hayward, A., & Rodrigues, L. C. (2007).
Guillain-Barr´ syndrome and preceding infection with Campylobacter , influenza and
Epstein-Barr virus in the general practice research database. PLoS One , 2 , e344.
Tarricone, C., Galizzi, A., Coda, A., Ascenzi, P., & Bolognesi, M. (1997). Unusual structure
of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp. Struc-
ture , 5 , 497-507.
Thomas, M. T., Shepherd, M., Poole, R. K., van Vliet, A. H., Kelly, D. J., & Pearson, B. M.
(2010). Two respiratory enzyme systems in Campylobacter jejun i NCTC 11168 contribute
to growth on L-lactate. Environmental Microbiology , 13 , 48-61.
Tsai, P. S., Kallio, P. T., & Bailey, J. E. (1995). Fnr, a global transcriptional regulator of
Escherichia coli , activates the vitreoscilla hemoglobin (VHb) promoter and intracellular