Matches in SemOpenAlex for { <https://semopenalex.org/work/W2744317860> ?p ?o ?g. }
- W2744317860 abstract "Iron-sulfur ([Fe-S]) clusters represent one of natures most diverse and ubiquitous protein prosthetic groups. [Fe-S] proteins are integral for diverse biological processes. Reconstitution of apo-proteins can occur by exogenously adding excess iron and sulfide. However, due to the toxicity of iron and sulfide, it is most likely that proteins coordinate [Fe-S] cluster assembly in cells. The first part of this dissertation addressed the iron donor for [Fe-S] cluster assembly. Recently, it has been shown that IscA is capable of binding iron with an association constant of 3.0 x 1019M-1. In addition, iron-loaded IscA is capable of donating iron to the proposed scaffold IscU for nascent [Fe-S] cluster assembly. We show that hIscA, the human homolog of E. coli IscA, functions as an iron chaperone for the assembly of [Fe-S] clusters in E. coli IscU. hIscA’s iron binding ability is similar to E. coli IscA. Moreover, hIscA is able to donate iron to IscU in the presence of 100-fold excess citrate, a metabolite capable of binding iron. This comparison signifies that [Fe-S] cluster assembly is conserved from bacteria to humans. The second part of this dissertation determined the participation of Ferritin A (FtnA) in [Fe-S] cluster assembly. FtnA, the major iron storage protein in E. coli, could serve as an iron reservoir when intracellular iron is depleted. We have shown that FtnA is capable of buffering iron when oxidative stress disrupts nascent [Fe-S] clusters and alleviates the production of hydroxyl radicals. Moreover, when physiological conditions return, IscA is able to retrieve iron from FtnA for [Fe-S] cluster assembly. The final part of this dissertation corroborated the interrelatedness of the oxidative and nitrosative stress response pathways. NsrR, a nitric oxide (NO) sensitive transcriptional repressor, is shown to coordinate a redox active [2Fe-2S] cluster with a midpoint redox potential of -346 ± 7 mV. The NsrR [2Fe-2S] cluster reacts with NO more quickly than other [Fe-S] proteins, signifying its role as a NO sensor. Finally, modification of the NsrR [2Fe-2S] cluster by NO results in the formation of a protein-bound dinitrosyl iron complex, relieving its DNA binding ability as a repressor." @default.
- W2744317860 created "2017-08-17" @default.
- W2744317860 creator A5080843946 @default.
- W2744317860 date "2022-06-10" @default.
- W2744317860 modified "2023-10-15" @default.
- W2744317860 title "Biogenesis of iron-sulfur clusters and intracellular iron metabolism" @default.
- W2744317860 cites W100311329 @default.
- W2744317860 cites W138169624 @default.
- W2744317860 cites W1437168237 @default.
- W2744317860 cites W1478455636 @default.
- W2744317860 cites W1486766426 @default.
- W2744317860 cites W1489620726 @default.
- W2744317860 cites W1509563342 @default.
- W2744317860 cites W1518212245 @default.
- W2744317860 cites W1518619062 @default.
- W2744317860 cites W1521463767 @default.
- W2744317860 cites W1525105770 @default.
- W2744317860 cites W1525976258 @default.
- W2744317860 cites W1526995501 @default.
- W2744317860 cites W1532066573 @default.
- W2744317860 cites W1532421291 @default.
- W2744317860 cites W154625286 @default.
- W2744317860 cites W1550904083 @default.
- W2744317860 cites W1551307287 @default.
- W2744317860 cites W1554568866 @default.
- W2744317860 cites W1555666244 @default.
- W2744317860 cites W1565852815 @default.
- W2744317860 cites W1568462943 @default.
- W2744317860 cites W1578537067 @default.
- W2744317860 cites W1581168206 @default.
- W2744317860 cites W1583466237 @default.
- W2744317860 cites W1585939084 @default.
- W2744317860 cites W1589307419 @default.
- W2744317860 cites W1589564633 @default.
- W2744317860 cites W1590567489 @default.
- W2744317860 cites W1621595817 @default.
- W2744317860 cites W1626591090 @default.
- W2744317860 cites W1646462907 @default.
- W2744317860 cites W1650974279 @default.
- W2744317860 cites W1655445995 @default.
- W2744317860 cites W168078121 @default.
- W2744317860 cites W1691960140 @default.
- W2744317860 cites W169202639 @default.
- W2744317860 cites W1845403835 @default.
- W2744317860 cites W1864334248 @default.
- W2744317860 cites W1888056390 @default.
- W2744317860 cites W1910268468 @default.
- W2744317860 cites W191322441 @default.
- W2744317860 cites W1947935290 @default.
- W2744317860 cites W1958309861 @default.
- W2744317860 cites W1960048856 @default.
- W2744317860 cites W1963777377 @default.
- W2744317860 cites W1965079356 @default.
- W2744317860 cites W1965295255 @default.
- W2744317860 cites W1965332062 @default.
- W2744317860 cites W1966132636 @default.
- W2744317860 cites W1966517868 @default.
- W2744317860 cites W1966631359 @default.
- W2744317860 cites W1966653175 @default.
- W2744317860 cites W1966999937 @default.
- W2744317860 cites W1967298352 @default.
- W2744317860 cites W1968304070 @default.
- W2744317860 cites W1968458406 @default.
- W2744317860 cites W1968915476 @default.
- W2744317860 cites W1969184431 @default.
- W2744317860 cites W1969756310 @default.
- W2744317860 cites W1969887535 @default.
- W2744317860 cites W1972740600 @default.
- W2744317860 cites W1973968247 @default.
- W2744317860 cites W1974086171 @default.
- W2744317860 cites W1975551775 @default.
- W2744317860 cites W1975664234 @default.
- W2744317860 cites W1976321043 @default.
- W2744317860 cites W1976522531 @default.
- W2744317860 cites W1976545490 @default.
- W2744317860 cites W1976619439 @default.
- W2744317860 cites W1977624070 @default.
- W2744317860 cites W1977671794 @default.
- W2744317860 cites W1978663690 @default.
- W2744317860 cites W1978679164 @default.
- W2744317860 cites W1979243834 @default.
- W2744317860 cites W1979289669 @default.
- W2744317860 cites W1979650977 @default.
- W2744317860 cites W1979991828 @default.
- W2744317860 cites W1980009425 @default.
- W2744317860 cites W1980964234 @default.
- W2744317860 cites W1981365590 @default.
- W2744317860 cites W1981376769 @default.
- W2744317860 cites W1982245868 @default.
- W2744317860 cites W1982468922 @default.
- W2744317860 cites W1983081312 @default.
- W2744317860 cites W1983644317 @default.
- W2744317860 cites W1984104940 @default.
- W2744317860 cites W1984882823 @default.
- W2744317860 cites W1984963076 @default.
- W2744317860 cites W1984978561 @default.
- W2744317860 cites W1985844569 @default.
- W2744317860 cites W1986962297 @default.
- W2744317860 cites W1987802907 @default.
- W2744317860 cites W1988891184 @default.