Literature DB >> 6938971

A new approach to time-resolved studies of ATP-requiring biological systems; laser flash photolysis of caged ATP.

J A McCray, L Herbette, T Kihara, D R Trentham.   

Abstract

2-Nitrobenzyl derivatives have been used for several years as photolabile protecting groups in synthetic organic chemistry. Recently, P3-1-(2-nitro phenylethyladenosine 5'-triphosphate "caged ATP" was synthesized and its photolysis was shown to generate ATP in situ. This and related reactions have great potential for structural and kinetic studies of both intact and soluble biological systems and it is thus important to define the kinetic characteristics of the photolytic reaction. Caged ATP (2.5 mM) was photolyzed at 347 nm by a single 30-nsec pulse from a frequency-doubled ruby laser of 25 mJ energy to generate 500 microM ATP. The kinetics of the overall reaction were determined by monitoring the kinetics of ATP-induced dissociation of actomyosin, a reaction of known kinetic characteristics. Release of 500 microM ATP was found to be controlled by a process having a rate constant of 2.2 X 10(9) [H+] sec-1 at 22 degrees C at pH 5.8-9.5, which corresponds to 220 sec-1 at pH 7. This process is believed to be the breakdown of an aci-nitro compound, which was identified on the basis of its spectral properties and the photochromicity of related 2-nitrobenzyl compounds.

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Year:  1980        PMID: 6938971      PMCID: PMC350477          DOI: 10.1073/pnas.77.12.7237

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  10 in total

1.  The photochemical formation of a quickly reacting form of haemoglobin.

Authors:  Q H GIBSON
Journal:  Biochem J       Date:  1959-02       Impact factor: 3.857

2.  Mechanism of actomyosin adenosine triphosphatase. Evidence that adenosine 5'-triphosphate hydrolysis can occur without dissociation of the actomyosin complex.

Authors:  L A Stein; R P Schwarz; P B Chock; E Eisenberg
Journal:  Biochemistry       Date:  1979-09-04       Impact factor: 3.162

3.  Determination of the association of myosin subfragment 1 with actin in the presence of ATP.

Authors:  P D Wagner; A G Weeds
Journal:  Biochemistry       Date:  1979-05-29       Impact factor: 3.162

4.  Rapid photolytic release of adenosine 5'-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts.

Authors:  J H Kaplan; B Forbush; J F Hoffman
Journal:  Biochemistry       Date:  1978-05-16       Impact factor: 3.162

5.  Light-activated drug confirms a mechanism of ion channel blockade.

Authors:  H A Lester; M E Krouse; M M Nass; N H Wassermann; B F Erlanger
Journal:  Nature       Date:  1979-08-09       Impact factor: 49.962

6.  Studies on the kinetics of formation and dissociation of the actomyosin complex.

Authors:  B Finlayson; R W Lymn; E W Taylor
Journal:  Biochemistry       Date:  1969-03       Impact factor: 3.162

7.  Oxygen recombination kinetics following laser photolysis of oxyhemoglobin.

Authors:  J A McCray
Journal:  Biochem Biophys Res Commun       Date:  1972-04-14       Impact factor: 3.575

8.  Intrinsic fluorescence of actin.

Authors:  S S Lehrer; G Kerwar
Journal:  Biochemistry       Date:  1972-03-28       Impact factor: 3.162

9.  Synthesis, structure, and reactivity of adenosine cyclic 3',5'-phosphate benzyl triesters.

Authors:  J Engels; E J Schlaeger
Journal:  J Med Chem       Date:  1977-07       Impact factor: 7.446

10.  Selective purification of the thiol peptides of myosin.

Authors:  A G Weeds; B S Hartley
Journal:  Biochem J       Date:  1968-04       Impact factor: 3.857

  10 in total
  73 in total

1.  Na(+) transport, and the E(1)P-E(2)P conformational transition of the Na(+)/K(+)-ATPase.

Authors:  A Babes; K Fendler
Journal:  Biophys J       Date:  2000-11       Impact factor: 4.033

2.  Time-resolved charge movements in the sarcoplasmatic reticulum Ca-ATPase.

Authors:  Christine Peinelt; Hans-Jürgen Apell
Journal:  Biophys J       Date:  2004-02       Impact factor: 4.033

3.  Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: a time-resolved infrared difference study.

Authors:  Begoña Sot; Fritzthof von Germar; Werner Mäntele; Jose María Valpuesta; Stefka G Taneva; Arturo Muga
Journal:  Protein Sci       Date:  2005-08-04       Impact factor: 6.725

4.  Microtubule assembly and oscillations induced by flash photolysis of caged-GTP.

Authors:  A Marx; A Jagla; E Mandelkow
Journal:  Eur Biophys J       Date:  1990       Impact factor: 1.733

5.  Charge translocation by the Na,K-pump: I. Kinetics of local field changes studied by time-resolved fluorescence measurements.

Authors:  R Bühler; W Stürmer; H J Apell; P Läuger
Journal:  J Membr Biol       Date:  1991-04       Impact factor: 1.843

6.  Time-Resolved Structural Studies on Insect Flight Muscle after Photolysis of Caged-ATP.

Authors:  G Rapp; K J Poole; Y Maeda; K Güth; J Hendrix; R S Goody
Journal:  Biophys J       Date:  1986-11       Impact factor: 4.033

7.  Structural changes in the catalytic cycle of the Na+,K+-ATPase studied by infrared spectroscopy.

Authors:  Michael Stolz; Erwin Lewitzki; Rolf Bergbauer; Werner Mäntele; Ernst Grell; Andreas Barth
Journal:  Biophys J       Date:  2009-04-22       Impact factor: 4.033

8.  Shining a light on post-translational modification.

Authors:  Nigel G J Richards
Journal:  HFSP J       Date:  2008-03-12

9.  Restoring forces in cardiac myocytes. Insight from relaxations induced by photolysis of caged ATP.

Authors:  E Niggli; W J Lederer
Journal:  Biophys J       Date:  1991-05       Impact factor: 4.033

10.  Relaxation from rigor of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP.

Authors:  H Martin; R J Barsotti
Journal:  Biophys J       Date:  1994-04       Impact factor: 4.033

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