Special Issue "Physiological Sensors of Gases, Light, Redox State and Hypoxia"

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A special issue of Biosensors (ISSN 2079-6374).

Deadline for manuscript submissions: closed (30 April 2013)

Special Issue Editor

Guest Editor
Prof. Dr. James D. Satterlee (Website)

Department of Chemistry, Washington State University, Pullman, WA 99164-4630, USA
Fax: +1 509 335 8867
Interests: structure, function and dynamics of heme-enzyme small molecule sensors; PAS domain sensing and signaling proteins; globin-coupled sensor proteins; molecular engineering, NMR, X-ray crystallography, and mass spectrometry thereof

Special Issue Information

Dear Colleagues,

The past dozen years have witnessed increasing awareness of, and appreciation for the role played by protein biosensors in regulating physiological processes of organisms ranging from bacteria to mammals. It is the goal of this special issue of Biosensors to provide a forum focusing on recent research in several important areas in which naturally occurring protein biosensors control physiological processes. The scope of this issue encompasses physiological processes in any living organism. Specifically, this issue will preferentially focus on those biosensors that sense molecular gases, light, redox status and hypoxia. These broad topics will be defined by review articles targeting specific topics like NO-sensing, CO-sensing, O2-Sensing, globin-coupled sensors, sensors of hypoxia, light sensing and redox sensing. It is expected that the review articles will provide succinct backgrounds and perhaps serve as fora for critical discussions of each topic. Submission of contributed manuscripts in any of these areas is enthusiastically encouraged. Original research articles are particularly welcome, but articles containing critical analyses of existing information are also acceptable.

Prof. Dr. James D. Satterlee
Guest Editor

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biosensors is an international peer-reviewed Open Access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 300 CHF (Swiss Francs). English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.

Keywords

  • light-sensing
  • gas-sensing
  • NO-sensing
  • CO-sensing
  • O2-sensing
  • redox-sensing
  • hypoxia-sensing
  • protein biosensors
  • physiological sensors

Published Papers (2 papers)

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Review

Open AccessReview The DosS-DosT/DosR Mycobacterial Sensor System
Biosensors 2013, 3(3), 259-282; doi:10.3390/bios3030259
Received: 21 May 2013 / Revised: 15 June 2013 / Accepted: 26 June 2013 / Published: 4 July 2013
Cited by 7 | PDF Full-text (923 KB) | HTML Full-text | XML Full-text
Abstract
DosS/DosR is a two-component regulatory system in which DosS, a heme-containing sensor also known as DevS, under certain conditions undergoes autophosphorylation and then transfers the phosphate to DosR, a DNA-binding protein that controls the entry of Mycobacterium tuberculosis and other mycobacteria into [...] Read more.
DosS/DosR is a two-component regulatory system in which DosS, a heme-containing sensor also known as DevS, under certain conditions undergoes autophosphorylation and then transfers the phosphate to DosR, a DNA-binding protein that controls the entry of Mycobacterium tuberculosis and other mycobacteria into a latent, dormant state. DosT, a second sensor closely related to DosS, is present in M. tuberculosis and participates in the control of the dormancy response mediated by DosR. The binding of phosphorylated DosR to DNA initiates the expression of approximately fifty dormancy-linked genes. DosT is accepted to be a gas sensor that is activated in the ferrous state by the absence of an oxygen ligand or by the binding of NO or CO. DosS functions in a similar fashion as a gas sensor, but contradictory evidence has led to the suggestion that it also functions as a redox state sensor. This review focuses on the structure, biophysical properties, and function of the DosS/DosT heme sensors. Full article
(This article belongs to the Special Issue Physiological Sensors of Gases, Light, Redox State and Hypoxia)
Figures

Open AccessReview The Heme-Based Oxygen-Sensor Phosphodiesterase Ec DOS (DosP): Structure-Function Relationships
Biosensors 2013, 3(2), 211-237; doi:10.3390/bios3020211
Received: 24 April 2013 / Revised: 24 May 2013 / Accepted: 13 June 2013 / Published: 17 June 2013
Cited by 8 | PDF Full-text (699 KB) | HTML Full-text | XML Full-text
Abstract
Escherichia coli Direct Oxygen Sensor (Ec DOS, also known as Ec DosP) is a heme-based O2-sensing phosphodiesterase from Escherichia coli that catalyzes the conversion of cyclic-di-GMP to linear di-GMP. Cyclic-di-GMP is an important second messenger in bacteria, highlighting the [...] Read more.
Escherichia coli Direct Oxygen Sensor (Ec DOS, also known as Ec DosP) is a heme-based O2-sensing phosphodiesterase from Escherichia coli that catalyzes the conversion of cyclic-di-GMP to linear di-GMP. Cyclic-di-GMP is an important second messenger in bacteria, highlighting the importance of understanding structure-function relationships of Ec DOS. Ec DOS is composed of an N-terminal heme-bound O2-sensing PAS domain and a C-terminal phosphodiesterase catalytic domain. Notably, its activity is markedly enhanced by O2 binding to the heme Fe(II) complex in the PAS sensor domain. X-ray crystal structures and spectroscopic and catalytic characterization of the wild-type and mutant proteins have provided important structural and functional clues to understanding the molecular mechanism of intramolecular catalytic regulation by O2 binding. This review summarizes the intriguing findings that have obtained for Ec DOS. Full article
(This article belongs to the Special Issue Physiological Sensors of Gases, Light, Redox State and Hypoxia)

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