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characterisation is consistent with the involvement of this globin in
peroxidase-like chemistry. Additional analyses will be required to confi-
dently assign a functional role for this class III-truncated globin.
Given that cgb and ctb are members of the same regulon and their
upregulation is linked to nitrosative stress (via NssR), an integrated response
involving Cgb and Ctb has been suggested. Unravelling the molecular
mechanisms, controlling the cofactor/ligand-binding capabilities of NssR
may contribute towards the elucidation of the molecular switch that initiates
the response of Campylobacter to nitrosative stress under aerobic conditions.
However, mechanisms that confer NO tolerance during oxygen limitation
remain to be identified. Given the host of biochemical, biophysical and
genetic tools available to study the globins of Campylobacter , these evasive
mechanistic details will inevitably reveal themselves upon interrogation
via a multi-pronged approach.
ACKNOWLEDGEMENTS
The authors wish to thank the Consejo Nacional de Ciencia y Tecnologia (Mexico) for aid
through Grant number 99171 and Consejo Estatal de Ciencia, Tecnolog´a e Innovaci´nde
Michoac´n through Grant number 007 (Mariana Tinajero-Trejo).
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