Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1804, Issue 1, Pages 166-172Publisher
ELSEVIER
DOI: 10.1016/j.bbapap.2009.09.028
Keywords
Diguanylate cyclase; Oxygen sensor protein; Globin-coupled sensor; Heme; Bacterial second messenger
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Funding
- Japan Society for the Promotion of Science [19370059, 19770119]
- The Ministry of Education, Culture, Sports, Science and Technology [19045031, 21026033]
- Takeda Science Foundation
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We have studied the structural and enzymatic properties of a diguanylate cyclase from an obligatory anaerobic bacterium Desulfotalea psychrophila, which consists of the N-terminal sensor domain and the C-terminal diguanylate cyclase domain. The sensor domain shows an amino acid sequence homology and spectroscopic properties similar to those of the sensor domains of the globin-coupled sensor proteins containing a protoheme. This heme-containing diguanylate cyclase catalyzes the formation of cyclic di-GMP from GTP only when the heme in the sensor domain binds molecular oxygen. When the heme is in the ferric, deoxy, CO-bound, or NO-bound forms, no enzymatic activity is observed. Resonance Raman spectroscopy reveals that Tyr55 forms a hydrogen bond with the heme-bound O-2, but not with CO. Instead, Gln81 interacts with the heme-bound CO. These differences of a hydrogen bonding network will play a crucial role for the selective O-2 sensing responsible for the regulation of the enzymatic activity. (C) 2009 Elsevier B.V. All rights reserved.
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