Serine 363 of a hydrophobic region of Archaeal ribulose 1,5-bisphosphate carboxylase/oxygenase from <i>Archaeoglobus fulgidus</i> and <i>Thermococcus kodakaraensis</i> affects CO<sub>2</sub>/O<sub>2</sub> substrate specificity and oxygen sensitivity [electronic resource]
Ribulose-1,5-Bisphosphate Carboxylase Oxygenase; Oxygen; Enzymes; Complement System; Enzyme Structure; Crystal Structure; Enzyme Assays; Recombinant Proteins.
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| Online Access: |
Online Access (via OSTI) |
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| Corporate Author: | |
| Format: | Government Document Electronic eBook |
| Language: | English |
| Published: |
Washington, D.C. : Oak Ridge, Tenn. :
United States. Department of Energy. Office of Basic Energy Sciences ; distributed by the Office of Scientific and Technical Information, U.S. Department of Energy,
2015.
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| Subjects: |
| Summary: | Ribulose-1,5-Bisphosphate Carboxylase Oxygenase; Oxygen; Enzymes; Complement System; Enzyme Structure; Crystal Structure; Enzyme Assays; Recombinant Proteins. |
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| Abstract: | Archaeal ribulose 1, 5-bisphospate carboxylase/oxygenase (RubisCO) is differentiated from other RubisCO enzymes and is classified as a form III enzyme, as opposed to the form I and form II RubisCOs typical of chemoautotrophic bacteria and prokaryotic and eukaryotic phototrophs. The form III enzyme from archaea is particularly interesting as several of these proteins exhibit unusual and reversible sensitivity to molecular oxygen, including the enzyme from <i>Archaeoglobus fulgidus</i>. Previous studies with <i>A. fulgidus</i> RbcL2 had shown the importance of Met-295 in oxygen sensitivity and pointed towards the potential significance of another residue (Ser-363) found in a hydrophobic pocket that is conserved in all RubisCO proteins. In the current study, further structure/function studies have been performed focusing on Ser-363 of <i>A. fulgidus</i> RbcL2; various changes in this and other residues of the hydrophobic pocket point to and definitively establish the importance of Ser-363 with respect to interactions with oxygen. In addition, previous findings had indicated discrepant CO<sub>2</sub>/O<sub>2</sub> specificity determinations of the <i>Thermococcus kodakaraensis</i> RubisCO, a close homolog of A. fulgidus RbcL2. As a result, it is shown here that the <i>T. kodakaraensis</i> enzyme exhibits a similar substrate specificity as the <i>A. fulgidus</i> enzyme and is also oxygen sensitive, with equivalent residues involved in oxygen interactions. |
| Item Description: | Published through SciTech Connect. 09/18/2015. PLoS ONE 10 9 ISSN 1932-6203 AM. Nathan E. Kreel; F. Robert Tabita; Ivan Berg. |
| Physical Description: | Article No. e0138351 : digital, PDF file. |