Raman difference spectroscopy and the energetics of enzymatic catalysis

Robert Callender, Hua Deng, Donald Sloan, John Burgner, Kwok To Yue

Research output: Contribution to journalConference article

7 Citations (Scopus)

Abstract

We have thus shown the use of OMA Raman spectrometers, with some special precautions, are capable of measuring difference spectra to fairly high subtraction accuracy. In our studies on the dehydrogenases, we have reported results on cofactors and substrates bound to these enzymes. We have obtained the Raman signals from groups like the nucleotide, adenine, phosphate moieties, single carbonyl moieties, and so forth when bound to ca. 40000 molecular weight proteins. It seems clear that this technique is capable of measuring not only bound molecules, but signals of specific protein residues. For example, a particular residue may be isotopically labelled or changed into another using the techniques of protein engineering. Subtracting the spectrum of the native protein from that of the modified protein would yield the spectrum of the chosen residue. Moreover, there seems no reason that small groups in other macromolecular systems, like nucleic acid assemblies, could not be studied using the same methodology.

Original languageEnglish (US)
Pages (from-to)154-160
Number of pages7
JournalProceedings of SPIE - The International Society for Optical Engineering
Volume1057
DOIs
StatePublished - May 8 1989
EventBiomolecular Spectroscopy 1989 - Los Angeles, United States
Duration: Jan 15 1989Jan 20 1989

Fingerprint

Catalysis
Raman
catalysis
Spectroscopy
proteins
Proteins
Protein
spectroscopy
Cofactor
accident prevention
dehydrogenases
Adenine Nucleotides
Nucleic acids
adenines
nucleotides
nucleic acids
Subtraction
Nucleotides
Phosphate
Spectrometer

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Computer Science Applications
  • Applied Mathematics
  • Electrical and Electronic Engineering

Cite this

Raman difference spectroscopy and the energetics of enzymatic catalysis. / Callender, Robert; Deng, Hua; Sloan, Donald; Burgner, John; Yue, Kwok To.

In: Proceedings of SPIE - The International Society for Optical Engineering, Vol. 1057, 08.05.1989, p. 154-160.

Research output: Contribution to journalConference article

@article{7b8e6f4a43954ff792cb6569e680183f,
title = "Raman difference spectroscopy and the energetics of enzymatic catalysis",
abstract = "We have thus shown the use of OMA Raman spectrometers, with some special precautions, are capable of measuring difference spectra to fairly high subtraction accuracy. In our studies on the dehydrogenases, we have reported results on cofactors and substrates bound to these enzymes. We have obtained the Raman signals from groups like the nucleotide, adenine, phosphate moieties, single carbonyl moieties, and so forth when bound to ca. 40000 molecular weight proteins. It seems clear that this technique is capable of measuring not only bound molecules, but signals of specific protein residues. For example, a particular residue may be isotopically labelled or changed into another using the techniques of protein engineering. Subtracting the spectrum of the native protein from that of the modified protein would yield the spectrum of the chosen residue. Moreover, there seems no reason that small groups in other macromolecular systems, like nucleic acid assemblies, could not be studied using the same methodology.",
author = "Robert Callender and Hua Deng and Donald Sloan and John Burgner and Yue, {Kwok To}",
year = "1989",
month = "5",
day = "8",
doi = "10.1117/12.951658",
language = "English (US)",
volume = "1057",
pages = "154--160",
journal = "Proceedings of SPIE - The International Society for Optical Engineering",
issn = "0277-786X",
publisher = "SPIE",

}

TY - JOUR

T1 - Raman difference spectroscopy and the energetics of enzymatic catalysis

AU - Callender, Robert

AU - Deng, Hua

AU - Sloan, Donald

AU - Burgner, John

AU - Yue, Kwok To

PY - 1989/5/8

Y1 - 1989/5/8

N2 - We have thus shown the use of OMA Raman spectrometers, with some special precautions, are capable of measuring difference spectra to fairly high subtraction accuracy. In our studies on the dehydrogenases, we have reported results on cofactors and substrates bound to these enzymes. We have obtained the Raman signals from groups like the nucleotide, adenine, phosphate moieties, single carbonyl moieties, and so forth when bound to ca. 40000 molecular weight proteins. It seems clear that this technique is capable of measuring not only bound molecules, but signals of specific protein residues. For example, a particular residue may be isotopically labelled or changed into another using the techniques of protein engineering. Subtracting the spectrum of the native protein from that of the modified protein would yield the spectrum of the chosen residue. Moreover, there seems no reason that small groups in other macromolecular systems, like nucleic acid assemblies, could not be studied using the same methodology.

AB - We have thus shown the use of OMA Raman spectrometers, with some special precautions, are capable of measuring difference spectra to fairly high subtraction accuracy. In our studies on the dehydrogenases, we have reported results on cofactors and substrates bound to these enzymes. We have obtained the Raman signals from groups like the nucleotide, adenine, phosphate moieties, single carbonyl moieties, and so forth when bound to ca. 40000 molecular weight proteins. It seems clear that this technique is capable of measuring not only bound molecules, but signals of specific protein residues. For example, a particular residue may be isotopically labelled or changed into another using the techniques of protein engineering. Subtracting the spectrum of the native protein from that of the modified protein would yield the spectrum of the chosen residue. Moreover, there seems no reason that small groups in other macromolecular systems, like nucleic acid assemblies, could not be studied using the same methodology.

UR - http://www.scopus.com/inward/record.url?scp=8944246936&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=8944246936&partnerID=8YFLogxK

U2 - 10.1117/12.951658

DO - 10.1117/12.951658

M3 - Conference article

AN - SCOPUS:8944246936

VL - 1057

SP - 154

EP - 160

JO - Proceedings of SPIE - The International Society for Optical Engineering

JF - Proceedings of SPIE - The International Society for Optical Engineering

SN - 0277-786X

ER -