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A comparative study of the structura...

Utah State University., Chemistry and Biochemistry.

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A comparative study of the structural features and kinetic properties of the molybdenum-iron and vanadium-iron proteins from Azotobacter vinelandii.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	A comparative study of the structural features and kinetic properties of the molybdenum-iron and vanadium-iron proteins from Azotobacter vinelandii./
作者:	Pabon Sanclemente, Miguel Alejandro.
面頁冊數:	163 p.
附註:	Adviser: Lance C. Seefeldt.
Contained By:	Masters Abstracts International47-04.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=1462050
ISBN:	9781109007596

A comparative study of the structural features and kinetic properties of the molybdenum-iron and vanadium-iron proteins from Azotobacter vinelandii.
Pabon Sanclemente, Miguel Alejandro.

A comparative study of the structural features and kinetic properties of the molybdenum-iron and vanadium-iron proteins from Azotobacter vinelandii. - 163 p.

Adviser: Lance C. Seefeldt.

Thesis (M.S.)--Utah State University, 2009.

The work presented herein provides information with which to compare and contrast biological nitrogen fixation as catalyzed by the Mo- and V-nitrogenases from Azotobacter vinelandii.

ISBN: 9781109007596Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

A comparative study of the structural features and kinetic properties of the molybdenum-iron and vanadium-iron proteins from Azotobacter vinelandii.
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020 $a 9781109007596
035 $a (UMI)AAI1462050
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040 $a UMI $c UMI
100 1 $a Pabon Sanclemente, Miguel Alejandro. $3 1024139
245 1 2 $a A comparative study of the structural features and kinetic properties of the molybdenum-iron and vanadium-iron proteins from Azotobacter vinelandii.
300 $a 163 p.
500 $a Adviser: Lance C. Seefeldt.
500 $a Source: Masters Abstracts International, Volume: 47-04, page: 2195.
502 $a Thesis (M.S.)--Utah State University, 2009.
520 $a The work presented herein provides information with which to compare and contrast biological nitrogen fixation as catalyzed by the Mo- and V-nitrogenases from Azotobacter vinelandii.
520 $a Biological nitrogen fixation is accomplished in the bacterium Azotobacter vinelandii by means of three metalloenzymes: The molybdenum, vanadium, and iron-only nitrogenase. The knowledge regarding biological nitrogen fixation has come from studies on the Mo-dependent reaction. However, the V- and Fe-only-dependent reduction of nitrogen remains largely unknown.
520 $a By using homology modeling techniques, the protein folds that contain the metal cluster active sites for the V- and Fe-only nitrogenases were constructed. The models uncovered similarities and differences existing among the nitrogenases regarding the identity of the amino acid residues lining pivotal structural features for the correct functioning of the proteins. These differences, could account for the differences in catalytic properties depicted by these enzymes.
520 $a The quaternary structure of the dinitrogenases also differs. Such component in the Mo-nitrogenase is an alpha2beta2 tetramer while for the V- an Fe-only nitrogenase is an alpha2beta 2delta2 hexamer. The latter enzymes are unable to reduce N2 in the absence of a functional delta subunit, yet they reduce H+ and the non-physiological substrate C2H 2. Therefore, the delta subunit is essential for V- and Fe-only dependent nitrogen fixation by a mechanism that still remains unknown. In attempt to understand why the delta subunit is essential for V-dependent N2 reduction from a structural stand point, this work presents the strategy followed to clone the vnfG gene and purify its expression product, the delta subunit. The purified protein was subjected to crystallization trials and used to stabilize a histidine-tagged VFe protein that would otherwise purify with low Fe2+ content and poor H+ and C2H2 reduction activities. The VFe preparation was used to conduct substrate reduction assays to assess: (i) The electron allocation patterns to each of the reduction products of the substrates C2H 2, N2, N2H4, and N3 -; and (ii) Inhibition patterns among substrate and inhibitor of the nitrogenase reaction. This work also reports on the effect N2H 4 and N3- has on the electron flux to the products of the C2H2 reduction.
590 $a School code: 0241.
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
710 2 $a Utah State University. $b Chemistry and Biochemistry. $3 1024138
773 0 $t Masters Abstracts International $g 47-04.
790 $a 0241
790 1 0 $a Ensign, Scott $e committee member
790 1 0 $a Hevel, Joan $e committee member
790 1 0 $a Seefeldt, Lance C., $e advisor
791 $a M.S.
792 $a 2009
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=1462050