Gas-Selective Catalytic Regulation by a Newly Identified Globin-Coupled Sensor Phosphodiesterase Containing an HD-GYP Domain from the Human Pathogen .

Globin-coupled sensors constitute an important family of heme-based gas sensors, an emerging class of heme proteins. In this study, we have identified and characterized a globin-coupled sensor phosphodiesterase containing an HD-GYP domain (GCS-HD-GYP) from the human pathogen , which is an emerging foodborne pathogen of increasing public health concern. The amino acid sequence encoded by the gene from indicated the presence of an N-terminal globin domain and a C-terminal HD-GYP domain, with HD-GYP domains shown previously to display phosphodiesterase activity toward bis(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP), a bacterial second messenger that regulates numerous important physiological functions in bacteria, including in bacterial pathogens.

A novel hybrid protein composed of superoxide-dismutase-active Cu(II) complex and lysozyme.

A novel hybrid protein composed of a superoxide dismutase-active Cu(II) complex (CuST) and lysozyme (CuST@lysozyme) was prepared. The results of the spectroscopic and electrochemical analyses confirmed that CuST binds to lysozyme. We determined the crystal structure of CuST@lysozyme at 0.

Bacterial hemerythrin domain-containing oxygen and redox sensors: Versatile roles for oxygen and redox signaling.

Hemerythrin is an oxygen-binding protein originally found in certain marine invertebrates. Oxygen reversibly binds at its non-heme diiron center, which consists of two oxo-bridged iron atoms bound to a characteristic conserved set of five His residues, one Glu residue, and one Asp residue. It was recently discovered that several bacteria utilize hemerythrin as an oxygen- and redox-sensing domain in responding to changes in cellular oxygen concentration or redox status, and immediately adapt to these environmental changes in order to maintain important physiological processes, including chemotaxis and c-di-GMP synthesis and degradation.

A century of Morita therapy: What has and has not changed.

We review the history of Morita therapy (MT), which has existed for over 100 years, and examine what has changed over that period and what has not. Classic MT, which was dependent on a highly strict therapeutic approach, gradually lost its pre-eminence, but at the same time, the fundamental theory of MT was refined. This theory came to be applied to current outpatient MT and adapted to inpatient MT.

Characterization of a Cobalt-Substituted Globin-Coupled Oxygen Sensor Histidine Kinase from sp. Fw109-5: Insights into Catalytic Regulation by Its Heme Coordination Structure.

Heme-based gas sensors are an emerging class of heme proteins. GcHK, a globin-coupled histidine kinase from sp. Fw109-5, is an oxygen sensor enzyme in which oxygen binding to Fe(II) heme in the globin sensor domain substantially enhances its autophosphorylation activity.