Literature DB >> 8346552

Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms.

W Mäntele1.   

Abstract

Infrared spectroscopic methods have been developed in the past decade to a sensitivity and selectivity which renders them useful for the study of enzyme function and enzyme reaction mechanisms. Originally developed as difference techniques for the investigation of light-induced reactions of photoreactive proteins, and matured in the field of bacteriorhodopsin and rhodopsin, they can now be used for the study of redox proteins by the use of electrochemical cells, or for the study of many different enzymes by the use of photolabile effector molecules. This brief review summarizes the currently available methods of infrared difference spectroscopy, the technical prerequisites, achievements and limitations.

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Year:  1993        PMID: 8346552     DOI: 10.1016/0968-0004(93)90186-q

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  26 in total

1.  Redox potential of the terminal quinone electron acceptor QB in photosystem II reveals the mechanism of electron transfer regulation.

Authors:  Yuki Kato; Ryo Nagao; Takumi Noguchi
Journal:  Proc Natl Acad Sci U S A       Date:  2015-12-29       Impact factor: 11.205

2.  Use of helper enzymes for ADP removal in infrared spectroscopic experiments: application to Ca2+-ATPase.

Authors:  Man Liu; Eeva-Liisa Karjalainen; Andreas Barth
Journal:  Biophys J       Date:  2005-02-24       Impact factor: 4.033

3.  The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.

Authors:  Fernando Moro; Vanesa Fernández-Sáiz; Arturo Muga
Journal:  Protein Sci       Date:  2005-12-29       Impact factor: 6.725

4.  Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase.

Authors:  C Roy D Lancaster; Ursula S Sauer; Roland Gross; Alexander H Haas; Jürgen Graf; Harald Schwalbe; Werner Mäntele; Jörg Simon; M Gregor Madej
Journal:  Proc Natl Acad Sci U S A       Date:  2005-12-27       Impact factor: 11.205

5.  Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy.

Authors:  X Jiang; E Zaitseva; M Schmidt; F Siebert; M Engelhard; R Schlesinger; K Ataka; R Vogel; J Heberle
Journal:  Proc Natl Acad Sci U S A       Date:  2008-08-21       Impact factor: 11.205

6.  Real-time molecular monitoring of chemical environment in obligate anaerobes during oxygen adaptive response.

Authors:  Hoi-Ying N Holman; Eleanor Wozei; Zhang Lin; Luis R Comolli; David A Ball; Sharon Borglin; Matthew W Fields; Terry C Hazen; Kenneth H Downing
Journal:  Proc Natl Acad Sci U S A       Date:  2009-06-16       Impact factor: 11.205

7.  Kinetic and vibrational isotope effects of proton transfer reactions in channelrhodopsin-2.

Authors:  Tom Resler; Bernd-Joachim Schultz; Víctor A Lórenz-Fonfría; Ramona Schlesinger; Joachim Heberle
Journal:  Biophys J       Date:  2015-07-21       Impact factor: 4.033

8.  In-cell infrared difference spectroscopy of LOV photoreceptors reveals structural responses to light altered in living cells.

Authors:  Lukas Goett-Zink; Jessica L Klocke; Lena A K Bögeholz; Tilman Kottke
Journal:  J Biol Chem       Date:  2020-06-24       Impact factor: 5.157

9.  Modified molecular interactions of the pheophytin and plastoquinone electron acceptors in photosystem II of chlorophyll D-containing Acaryochloris marina as revealed by FTIR spectroscopy.

Authors:  Yuko Sano; Kaichiro Endo; Tatsuya Tomo; Takumi Noguchi
Journal:  Photosynth Res       Date:  2015-01-06       Impact factor: 3.573

10.  Calculated vibrational properties of pigments in protein binding sites.

Authors:  Hari Prasad Lamichhane; Gary Hastings
Journal:  Proc Natl Acad Sci U S A       Date:  2011-06-13       Impact factor: 11.205

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