The Dos Family of Globin-Related Sensors Using PAS Domains to Accommodate Haem Acting as the Active Site for Sensing External Signals - Advances in Microbial Physiology - page 321

regulatory implications for heme-based sensors. Proceedings of the National Academy of Sci-
ences of the United States of America , 99 , 12771-12776.
Londer, Y. Y., Dementieva, I. S., D'Ausilio, C. A., Pokkuluri, P. R., & Schiffer, M. (2006).
Characterization of a c-type heme-containing PAS sensor domain from Geobacter
sulfurreducens representing a novel family of periplasmic sensors in Geobacteraceae and
other bacteria. FEMS Microbiology Letters , 258 , 173-181.
Lukat-Rodgers, G. S., Rexine, J. L., & Rodgers, K. R. (1998). Heme speciation in alkaline
ferric FixL and possible tyrosine involvement in the signal transduction pathway for reg-
ulation of nitrogen fixation. Biochemistry , 37 , 13543-13552.
Marina, A., Waldburger, C. D., & Hendrickson, W. A. (2005). Structure of the entire cyto-
plasmic portion of a sensor histidine-kinase protein. EMBO Journal , 24 , 4247-4259.
Marvin, K. A., Kerby, R. L., Youn, H., Roberts, G. P., & Burstyn, J. N. (2008). The tran-
scription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemopro-
tein that undergoes a redox-mediated ligand switch. Biochemistry , 47 , 9016-9028.
Miyatake, H., Kanai, M., Adachi, S., Nakamura, H., Tamura, K., Tanida, H., et al. (1999a).
Dynamic light-scattering and preliminary crystallographic studies of the sensor domain of
the haem-based oxygen sensor FixL from Rhizobium meliloti . Acta Crystallographica.
Section D, Biological Crystallography , 55 , 1215-1218.
Miyatake, H., Mukai, M., Adachi, S., Nakamura, H., Tamura, K., Iizuka, T., et al. (1999b).
Iron coordination structures of oxygen sensor FixL characterized by Fe K-edge extended
X-ray absorption fine structure and resonance Raman spectroscopy. The Journal of
Biological Chemistry , 274 , 23176-23184.
Miyatake, H., Mukai, M., Park, S. Y., Adachi, S., Tamura, K., Nakamura, H., et al. (2000).
Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti : Crystallographic,
mutagenesis and resonance Raman spectroscopic studies. Journal of Molecular Biology ,
301 , 415-431.
M¨glich, A., Ayers, R. A., & Moffat, K. (2009). Structure and signaling mechanism of Per-
ARNT-Sim domains. Structure , 17 , 1282-1294.
Monson, E. K., Ditta, G. S., & Helinski, D. R. (1995). The oxygen sensor protein, FixL, of
Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation, and
signal transduction. The Journal of Biological Chemistry , 270 , 5243-5250.
Mukai, M., Nakamura, K., Nakamura, H., Iizuka, T., & Shiro, Y. (2000). Roles of Ile209
and Ile210 on the heme pocket structure and regulation of histidine kinase activity of
oxygen sensor FixL from Rhizobium meliloti . Biochemistry , 39 , 13810-13816.
Mukai, M., Savard, P. Y., Ouellet, H., Guertin, M., & Yeh, S. R. (2002). Unique ligand-
protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis .
Biochemistry , 41 , 3897-3905.
Mukaiyama, Y., Uchida, T., Sato, E., Sasaki, A., Sato, Y., Igarashi, J., et al. (2006). Spectro-
scopic and DNA-binding characterization of the isolated heme-bound basic helix-loop-
helix-PAS-A domain of neuronal PAS protein 2 (NPAS2), a transcription activator
protein associated with circadian rhythms. FEBS Journal , 273 , 2528-2539.
Nakajima, H., Honma, Y., Tawara, T., Kato, T., Park, S. Y., Miyatake, H., et al. (2001).
Redox properties and coordination structure of the heme in the CO-sensing transcrip-
tional activator CooA. The Journal of Biological Chemistry , 276 , 7055-7061.
Nakajima, H., Takatani, N., Yoshimitsu, K., Itoh, M., Aono, S., Takahashi, Y., et al. (2010).
The role of the Fe-S cluster in the sensory domain of nitrogenase transcriptional activator
VnfA from Azotobacter vinelandii . FEBS Journal , 277 , 817-832.
Nakamura, H., Kumita, H., Imai, K., Iizuka, T., & Shiro, Y. (2004). ADP reduces the
oxygen-binding affinity of a sensory histidine kinase, FixL: The possibility of an
enhanced reciprocating kinase reaction. Proceedings of the National Academy of Sciences of
the United States of America , 101 , 2742-2746.