Dynamics of the Heme-binding Bacterial Gas-sensing Dissimilative Nitrate Respiration Regulator (DNR) and Activation Barriers for Ligand Binding and Escape

Lobato, Laura; Bouzhir-Sima, Latifa; Yamashita, Takahiro; Wilson, Michael T.; Vos, Marten H.; Liebl, Ursula

doi:10.1074/jbc.m114.571398

Cited by 27 publications

(44 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Ultrafast broad-band transient absorption experiments at a 500 Hz repetition rate, were performed as previously described 16 . Pump pulses centered at 520 or 570 nm were generated using a home-built, non-collinear optical parametric amplifier, and centered at 390 nm by frequency doubling of the fundamental beam.…”

Section: Methodsmentioning

confidence: 99%

Ultrafast photochemistry of the bc₁complex

Vos

Reeder

Daldal

et al. 2017

Phys. Chem. Chem. Phys.

Self Cite

View full text Add to dashboard Cite

We present a full investigation of ultrafast light-induced events in the membraneous cytochrome bc1 complex by transient absorption spectroscopy. This energy-transducing complex harbors four redox-active components per monomer: heme c1, two 6-coordinate b-hemes and a [2Fe-2S] cluster. Using excitation of these components in different ratios under various excitation conditions, probing in the full visible range and under three well-defined redox conditions, we demonstrate that for all ferrous hemes of the complex photodissociation of axial ligands takes place and that they rebind in 5–7 ps, as in other 6-coordinate heme proteins, including cytoglobin, which is included as a reference in this study. By contrast, the signals are not consistent with photooxidation of the b hemes. This conclusion contrasts with a recent assessment based on a more limited data set. The binding kinetics of internal and external ligands are indicative of a rigid heme environment, consistent with the electron transfer function. We also report, for the first time, photoactivity of the very weakly absorbing iron-sulfur center. This yields the unexpected perspective of studying photochemistry, initiated by excitation of iron-sulfur clusters, in a range of protein complexes.

show abstract

Section: Methodsmentioning

confidence: 99%

Ultrafast photochemistry of the bc₁complex

Vos

Reeder

Daldal

et al. 2017

Phys. Chem. Chem. Phys.

Self Cite

View full text Add to dashboard Cite

show abstract

“…In addition to Cys residues, iron is frequently used by regulatory proteins to sense O 2 , NO·, carbon monoxide (CO), O 2 · − , or redox cycling compounds. Iron can be found as (i) mononuclear centers in Fur, PerR (peroxide regulator) or NorR (nitric oxide regulator), (ii) [2Fe-2S] and [4Fe-4S] clusters in SoxR (superoxide regulator), FNR (fumarate-nitrate reduction regulator) or NsrR (nitric oxide-responsive regulator), or (iii) heme prosthetic groups in dormancy survival regulatory proteins DosT and DosS, or DNR (dissimilative nitrate respiration regulator) (Crack et al, 2014; Ji et al, 2015; Lobato et al, 2014; Ma et al, 2012). Molecular mechanisms of redox sensing rely on protein conformational changes triggered by interaction with reactive oxygen and nitrogen species (see accompanying review in this issue, Fang et al, 2016) (Figure 2B).…”

Section: Stresses In the Host Environmentmentioning

confidence: 99%

Bacterial Stress Responses during Host Infection

Fang

Frawley

Tapscott

et al. 2016

Cell Host & Microbe

262

224

View full text Add to dashboard Cite

Pathogenic bacteria must withstand diverse host environments during infection. Environmental signals, such as pH, temperature, nutrient scarcity, etc., not only trigger adaptive responses within bacteria to these specific stress conditions but also direct the expression of virulence genes at an appropriate time and place. An appreciation of stress responses and their regulation is therefore essential for an understanding of bacterial pathogenesis. This review considers specific stresses in the host environment and their relevance to pathogenesis, with a particular focus on the enteric pathogen Salmonella.

show abstract

“…The affinity of the DNR-NO complex for its cognate DNA was recently determined to be in the nanomolar range (50).…”

Section: Figmentioning

confidence: 99%

“…In this metabolic pathway, nitrate is reduced to NO and then to N 2 in four reaction steps, each catalyzed by a specific reductase ( Fig. 1) whose expression is tightly controlled, mainly by the arginine nitrate regulation (ANR) and dissimilative nitrate respiration regulator (DNR) transcription factors (48)(49)(50)(51)(52)(53). Two putative nitrate reductases are present in P. aeruginosa, i.e., the inner membranebound nitrate reductase NarGHI ( Fig.…”

Section: Endogenous Sources Of No In P Aeruginosa and Their Effects mentioning

confidence: 99%

Origin and Impact of Nitric Oxide in Pseudomonas aeruginosa Biofilms

Cutruzzolà

Frankenberg‐Dinkel

2016

J Bacteriol

View full text Add to dashboard Cite

bThe formation of the organized bacterial community called biofilm is a crucial event in bacterial physiology. Given that biofilms are often refractory to antibiotics and disinfectants to which planktonic bacteria are susceptible, their formation is also an industrially and medically relevant issue. Pseudomonas aeruginosa, a well-known human pathogen causing acute and chronic infections, is considered a model organism to study biofilms. A large number of environmental cues control biofilm dynamics in bacterial cells. In particular, the dispersal of individual cells from the biofilm requires metabolic and morphological reprogramming in which the second messenger bis-(3=-5=)-cyclic dimeric GMP (c-di-GMP) plays a central role. The diatomic gas nitric oxide (NO), a well-known signaling molecule in both prokaryotes and eukaryotes, is able to induce the dispersal of P. aeruginosa and other bacterial biofilms by lowering c-di-GMP levels. In this review, we summarize the current knowledge on the molecular mechanisms connecting NO sensing to the activation of c-di-GMP-specific phosphodiesterases in P. aeruginosa, ultimately leading to c-di-GMP decrease and biofilm dispersal. PSEUDOMONAS AERUGINOSA: A MODEL SYSTEM FOR BIOFILM RESEARCH

show abstract

Dynamics of the Heme-binding Bacterial Gas-sensing Dissimilative Nitrate Respiration Regulator (DNR) and Activation Barriers for Ligand Binding and Escape

Cited by 27 publications

References 56 publications

Ultrafast photochemistry of the bc₁complex

Ultrafast photochemistry of the bc₁complex

Bacterial Stress Responses during Host Infection

Origin and Impact of Nitric Oxide in Pseudomonas aeruginosa Biofilms

Contact Info

Product

Resources

About

Dynamics of the Heme-binding Bacterial Gas-sensing Dissimilative Nitrate Respiration Regulator (DNR) and Activation Barriers for Ligand Binding and Escape

Cited by 27 publications

References 56 publications

Ultrafast photochemistry of the bc1complex

Ultrafast photochemistry of the bc1complex

Bacterial Stress Responses during Host Infection

Origin and Impact of Nitric Oxide in Pseudomonas aeruginosa Biofilms

Contact Info

Product

Resources

About

Ultrafast photochemistry of the bc₁complex

Ultrafast photochemistry of the bc₁complex