U.S. flag

An official website of the United States government

Dot gov

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Https

Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.

PubAg

Main content area

You searched for: Subject spectroscopy Remove constraint Subject: spectroscopy Subject enzymology Remove constraint Subject: enzymology Subject term spectroscopy Remove constraint Subject term: spectroscopy Text Availability Citation in PubAg Remove constraint Text Availability: Citation in PubAg
Start Over

Search

8  Search Results

1 - 8 of 8
Number of results to display per page

Search Results

1. Cellular adaptation responses in a halotolerant Exiguobacterium exhibiting organic solvent tolerance with simultaneous protease production

Author:
Nitin Srivastava; Sumit Kumar; Sugathan Shiburaj; Anshu Gupta; Sunil Kumar Khare
Source:
Environmental technology & innovation 2021 v.23 pp. 101803
ISSN:
2352-1864
Subject:
Exiguobacterium; Gram-positive bacteria; biosynthesis; cell membranes; cost effectiveness; decane; environmental technology; enzymology; estuaries; heptane; hexane; hydrophobicity; iso-octanes; octane; peptides; permeability; proteinases; salt tolerance; sediments; solvents; spectroscopy; toxicity; viability
Abstract:
... Solvent tolerance is a novel trait among halotolerant bacteria and their enzymes. However, the solvent response mechanisms in Gram-positive bacteria remain less investigated. The Exiguobacterium indicum (TBG-PICH-001) was isolated from the sediment of Pichavaram estuary. It possessed halotolerance and could prove to be a suitable candidate for solvent tolerance studies. The present study extensive ...
DOI:
10.1016/j.eti.2021.101803

2. Structural Enzymology of Nitrogenase Enzymes

Author:
Oliver Einsle; Douglas C. Rees
Source:
Chemical reviews 2020 v.120 no.12 pp. 4969-5004
ISSN:
1520-6890
Subject:
active sites; ammonia; carbon; electrons; enzymology; hydrides; iron; ligands; models; nitrogen; nitrogenase; proteins; protons; reducing agents; spectroscopy
Abstract:
... The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography involving two component proteins, MgATP and reductant. At center stage of this process resides the active site cofactor, a complex metallocluster organized around a trigonal prismatic arrangement of iron sites surrounding an interstitial carbon. As a consequence of the choreography, electrons and protons are deli ...
DOI:
10.1021/acs.chemrev.0c00067

3. Ternary Complex Formation and Photoactivation of a Photoenzyme Results in Altered Protein Dynamics

Author:
Andreas Maximilian Stadler; Judith Schneidewind; Michaela Zamponi; Esther Knieps-Grünhagen; Samira Gholami; Ulrich Schwaneberg; Ivan Rivalta; Marco Garavelli; Mehdi D. Davari; Karl-Erich Jaeger; Ulrich Krauss
Source:
Journal of physical chemistry 2019 v.123 no.34 pp. 7372-7384
ISSN:
1520-5207
Subject:
NADP (coenzyme); apoproteins; binding sites; catalytic activity; chemical bonding; chlorophyll; enzymes; enzymology; hydrides; molecular dynamics; neutrons; protein structure; simulation models; spectroscopy; thermal stability
Abstract:
... The interplay between protein dynamics and catalysis remains a fundamental question in enzymology. We here investigate the ns-timescale dynamics of a light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR), a photoenzyme crucial for chlorophyll synthesis. LPORs catalyze the light-triggered trans addition of a hydride and a proton across the C17═C18 double bond of the chlorophyll precursor ...
DOI:
10.1021/acs.jpcb.9b06608

4. Ensemble and single-molecule biophysical characterization of D17.4 DNA aptamer–IgE interactions

Author:
Mohan-Vivekanandan Poongavanam; Lydia Kisley; Katerina Kourentzi; Christy F. Landes; Richard C. Willson
Source:
Biochimica et biophysica acta 2016 v.1864 no.1 pp. 154-164
ISSN:
1570-9639
Subject:
DNA; activation energy; dissociation; drugs; electrostatic interactions; enthalpy; entropy; enzymology; fluorescence; immunoglobulin E; ionic strength; kinetics; magnesium chloride; mutants; oligonucleotides; salt concentration; sodium chloride; spectroscopy; temperature
Abstract:
... The IgE-binding DNA aptamer 17.4 is known to inhibit the interaction of IgE with the high-affinity IgE Fc receptor FcεRI. While this and other aptamers have been widely used and studied, there has been relatively little investigation of the kinetics and energetics of their interactions with their targets, by either single-molecule or ensemble methods.The dissociation kinetics of the D17.4/IgE comp ...
DOI:
10.1016/j.bbapap.2015.08.008

5. Evaluation of possible inhibition of human liver drug metabolizing cytochromes P450 by two new acetylcholinesterase oxime-type reactivators

Author:
Alena Spicakova; Pavel Anzenbacher; Barbora Liskova; Kamil Kuca; Josef Fusek; Eva Anzenbacherova
Source:
Food and chemical toxicology 2016 v.88 pp. 100-104
ISSN:
0278-6915
Subject:
acetylcholinesterase; antidotes; cytochrome P-450; drug interactions; enzymology; humans; liver; oximes; risk; spectroscopy; toxicology
Abstract:
... Two non-symmetric bispyridine oxime – based reactivators of acetylcholinesterase enzyme (AChE), labeled as K027 (1-(4-carbamoylpyridinium)-3-(4-hydroxyiminomethylpyridinium)-propane dibromide) and K203 ((E)-1-(4- carbamoylpyridinium)-4-(4-hydroxyiminomethylpyridinium)-but-2-ene dibromide) were tested for their potential to inhibit activities of human liver microsomal cytochromes P450 (CYP). Both o ...
DOI:
10.1016/j.fct.2015.11.024

6. Sizing up single-molecule enzymatic conformational dynamics

Author:
H. Peter Lu
Source:
Chemical Society reviews 2014 v.43 no.4 pp. 1118-1143
ISSN:
1460-4744
Subject:
enzymatic reactions; enzymes; enzymology; spectroscopy; theoretical models
Abstract:
... Enzymatic reactions and related protein conformational dynamics are complex and inhomogeneous, playing crucial roles in biological functions. The relationship between protein conformational dynamics and enzymatic reactions has been a fundamental focus in modern enzymology. It is extremely difficult to characterize and analyze such complex dynamics in an ensemble-averaged measurement, especially wh ...
DOI:
10.1039/c3cs60191a

7. Mechanistic enzymology of serine palmitoyltransferase

Author:
Hiroko Ikushiro; Hideyuki Hayashi
Source:
Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1474-1480
ISSN:
1878-1454
Subject:
biosynthesis; pyridoxal phosphate; sphingolipids; spectroscopy; enzymology; serine C-palmitoyltransferase
Abstract:
... Serine palmitoyltransferase, which is one of the α-oxamine synthase family enzymes, catalyzes the condensation reaction of L-serine and palmitoyl-CoA to form 3-ketodihydrosphingosine, the first and rate-determining step of the sphingolipid biosynthesis. As with other α-oxamine synthase family enzymes, the catalytic reaction is composed of multiple elementary steps, and the mechanism to control the ...
DOI:
10.1016/j.bbapap.2011.02.005

8. Pyridoxal-5′-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases

Author:
Perry A. Frey; George H. Reed
Source:
Biochimica et biophysica acta 2011 v.1814 no.11 pp. 1548-1557
ISSN:
1878-1454
Subject:
active sites; catalysts; crystal structure; enzymes; enzymology; free radicals; isomerization; lysine; ornithine; pyridoxal; spectroscopy
Abstract:
... PLP catalyzes the 1,2 shifts of amino groups in free radical-intermediates at the active sites of amino acid aminomutases. Free radical forms of the substrates are created upon H atom abstractions carried out by the 5′-deoxyadenosyl radical. In most of these enzymes, the 5′-deoxyadenosyl radical is generated by an iron–sulfur cluster-mediated reductive cleavage of S-adenosyl-(S)-methionine. Howeve ...
DOI:
10.1016/j.bbapap.2011.03.005