Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin
The nitrite reductase activity of heme proteins plays key roles in physiology by producing nitric oxide under hypoxic conditions. Many heme proteins exhibit the ability to convert nitrite to nitric oxide at different rates that appear to reflect the protein environment of the heme moiety. We hypothe...
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San Francisco State University
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ftcalifstateuniv:oai:scholarworks:sx61dn76r 2024-09-30T14:44:15+00:00 Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin Lea Cassandra Lough Raymond Esquerra George Gassner Anton Guliaev 2012 http://hdl.handle.net/10211.3/122352 English eng San Francisco State University Science & Engineering Chemistry: Concentration in Biochemistry http://hdl.handle.net/10211.3/122352 Copyright by Lea Cassandra Lough, 2012 AS36 2012 CHEM .L68 Masters Thesis 2012 ftcalifstateuniv 2024-09-10T17:06:17Z The nitrite reductase activity of heme proteins plays key roles in physiology by producing nitric oxide under hypoxic conditions. Many heme proteins exhibit the ability to convert nitrite to nitric oxide at different rates that appear to reflect the protein environment of the heme moiety. We hypothesized that His 64 mutations to alanine (H64A), valine (H64V), leucine (H64L), and glutamine (H64Q) will alter the nitrite reductase rate by preventing the hydrogen bond to HNO2 . We also proposed that a decrease in distal pocket size with Leu 29 mutations to phenylalanine and tryptophan will decrease the rate of the reaction by limiting the accessibility of nitrite to the heme. To test these hypotheses, we spectrophotometrically measured the nitrite reductase activity of these mutants. Master Thesis Sperm whale Scholarworks from California State University |
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Scholarworks from California State University |
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ftcalifstateuniv |
language |
English |
description |
The nitrite reductase activity of heme proteins plays key roles in physiology by producing nitric oxide under hypoxic conditions. Many heme proteins exhibit the ability to convert nitrite to nitric oxide at different rates that appear to reflect the protein environment of the heme moiety. We hypothesized that His 64 mutations to alanine (H64A), valine (H64V), leucine (H64L), and glutamine (H64Q) will alter the nitrite reductase rate by preventing the hydrogen bond to HNO2 . We also proposed that a decrease in distal pocket size with Leu 29 mutations to phenylalanine and tryptophan will decrease the rate of the reaction by limiting the accessibility of nitrite to the heme. To test these hypotheses, we spectrophotometrically measured the nitrite reductase activity of these mutants. |
author2 |
Raymond Esquerra George Gassner Anton Guliaev |
format |
Master Thesis |
author |
Lea Cassandra Lough |
spellingShingle |
Lea Cassandra Lough Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin |
author_facet |
Lea Cassandra Lough |
author_sort |
Lea Cassandra Lough |
title |
Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin |
title_short |
Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin |
title_full |
Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin |
title_fullStr |
Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin |
title_full_unstemmed |
Effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin |
title_sort |
effects of distal pocket mutations on the nitrite reductase of sperm whale myoglobin |
publisher |
San Francisco State University |
publishDate |
2012 |
url |
http://hdl.handle.net/10211.3/122352 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
AS36 2012 CHEM .L68 |
op_relation |
http://hdl.handle.net/10211.3/122352 |
op_rights |
Copyright by Lea Cassandra Lough, 2012 |
_version_ |
1811645652410564608 |