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Abiotic Interactions and Redox Analysis in Manganese Oxidation by MopA-hp
Başlık:
Abiotic Interactions and Redox Analysis in Manganese Oxidation by MopA-hp
Yazar:
Rizo, Antonia, author.
ISBN:
9780438054387
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (57 pages)
Genel Not:
Source: Masters Abstracts International, Volume: 57-06M(E).
Advisors: Hope A. Johnson Committee members: Esther Chen; Madeline E. Rasche.
Özet:
The manganese oxidizing protein, MopA, from Erythrobacter sp. SD-21 is a heme peroxidase capable of manganese oxidation. Unlike other manganese oxidizing enzymes, understanding of MopA is limited. Heterologous expression and purification of the peroxidase domain from MopA, MopA-hp, leads to a protein sample with contaminants. The work presented shows that additional purification with the use of ATP-MgCl2 does not improve the overall protein purity. Using the partially purified MopA-hp, the roles of PQQ and NAD+, in manganese oxidation by the protein were analyzed through a series of spectrophotometric and kinetic analyses. The results indicate NAD+ reduction cannot be measured under the current conditions likely because of competing reactions with protein contaminants, manganese oxides and PQQ. In addition, spectrophotometric analysis suggests a binding interaction between NAD+ and manganese(II) is unlikely, while an interaction between PQQ and manganese(II) may occur. This interaction could play an important role in manganese(II) oxidation and could affect the electron potential of manganese(II) during manganese oxidation by MopA-hp.
Notlar:
School code: 6060
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Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(691095.1) | 691095-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
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