Os03g0233900 - Revision history

Rice2012: /* Structured Information */

2015-06-12T05:38:02Z

‎Structured Information

Wangjinlong: /* Annotated Information */

2014-06-09T15:56:38Z

‎Annotated Information

Wangjinlong: /* Annotated Information */

2014-06-09T15:52:34Z

‎Annotated Information

Wangjinlong: /* Annotated Information */

2014-06-09T15:51:49Z

‎Annotated Information

Wangjinlong: /* Annotated Information */

2014-06-09T15:45:20Z

‎Annotated Information

Wangjinlong: /* Annotated Information */

2014-06-09T15:44:07Z

‎Annotated Information

Wangjinlong: /* Function */

2014-06-07T07:43:16Z

‎Function

Wangjinlong: /* Function */

2014-06-07T07:42:11Z

‎Function

Wangjinlong: /* Function */

2014-06-07T07:41:11Z

‎Function

Wangjinlong: /* Function */

2014-06-07T07:40:34Z

‎Function

@@ Line 76: / Line 76: @@
 ==Structured Information==
 [[Category:Genes]]
 [[Category:Japonica mRNA]]

← Older revision		Revision as of 15:56, 9 June 2014
Line 42:		Line 42:

	Expressed in coleoptiles, embryos, leaves and roots By flooding and etiolating but not by oxidative, nitrosative or hormonal stresses.		Expressed in coleoptiles, embryos, leaves and roots By flooding and etiolating but not by oxidative, nitrosative or hormonal stresses.
		+
		+	These Hbs are not oxygen transporters and have hypothetical roles in nitrogen metabolism. The deoxyferrous forms of each react rapidly with nitrite to form ferric Hb and ferrous-nitrosyl Hb in a fixed ratio, indicative of the production of nitric oxide from the reduction of nitrite by ferrous Hb.<ref name='ref1' />

	deoxyferrous rice nsHb1 and SynHb convert HA specifically to ammonium at rates 100−2500 times faster than the animal Hbs. These results complement those of nitrite reduction by rice nsHb1 and SynHb and support the hypothesis that they serve as an alternative means of reducing nitrogen metabolites, recycling NADH produced during anaerobic glycolysis, and continuing ammonium production during hypoxia.<ref name='ref3' />		deoxyferrous rice nsHb1 and SynHb convert HA specifically to ammonium at rates 100−2500 times faster than the animal Hbs. These results complement those of nitrite reduction by rice nsHb1 and SynHb and support the hypothesis that they serve as an alternative means of reducing nitrogen metabolites, recycling NADH produced during anaerobic glycolysis, and continuing ammonium production during hypoxia.<ref name='ref3' />

@@ Line 43: / Line 43: @@
 Expressed in coleoptiles, embryos, leaves and roots By flooding and etiolating but not by oxidative, nitrosative or hormonal stresses.
-deoxyferrous rice nsHb1 and SynHb convert HA specifically to ammonium at rates 100−2500 times faster than the animal Hbs. These results complement those of nitrite reduction by rice nsHb1 and SynHb and support the hypothesis that they serve as an alternative means of reducing nitrogen metabolites, recycling NADH produced during anaerobic glycolysis, and continuing ammonium production during hypoxia.
+deoxyferrous rice nsHb1 and SynHb convert HA specifically to ammonium at rates 100−2500 times faster than the animal Hbs. These results complement those of nitrite reduction by rice nsHb1 and SynHb and support the hypothesis that they serve as an alternative means of reducing nitrogen metabolites, recycling NADH produced during anaerobic glycolysis, and continuing ammonium production during hypoxia.<ref name='ref3' />
 ===Evolution===

@@ Line 5: / Line 5: @@
 Hemoglobins (Hbs) with unknown functions have been found in most organisms. A hypothetical role common tomany of them is nitric oxide (NO) scavenging, which is grounded in the established contribution of Hbs to nitric oxide dioxygenase (HbO2 + NO == metHb + NO3-) (NOD) activity in bacterial flavohemoglobins, the effects of blood cell Hb on NO metabolism, and the general reactivity of oxy, deoxy, and ferric hemoglobins with NO. In plants, the NOD function for Hbs is supported by increases in the level of Hb expression in response to nitrate, nitrite, and nitric oxide, improvements in NO scavenging ability in plants overexpressing Hb, decreases in the levels of NO-sensitive enzymes in plants with down regulated Hb, and the encouragement of cell growth by cyanobacterial Hb in the presence of high concentrations of reactive nitrogen species.
 ===Function===
@@ Line 38: / Line 42: @@
 Expressed in coleoptiles, embryos, leaves and roots By flooding and etiolating but not by oxidative, nitrosative or hormonal stresses.
 ===Evolution===

@@ Line 14: / Line 14: @@
 The reactions of class 1 rice nonsymbiotic Hb (rice nsHb1) with nitrate and nitrite suggested that these Hbs are not oxygen transporters and have hypothetical roles in nitrogen metabolism. And the deoxyferrous forms of each react rapidly with nitrite to form ferric Hb and ferrous-nitrosyl Hb in a fixed ratio, indicative of the production of nitric oxide from the reduction of nitrite by ferrous Hb.<ref name="ref1"/>
-[[File: nshb1.GIF |center|thumb|'' Reaction of rice nsHb1 and SynHb with nitrite. The spectral changes associated with Rice nsHb1 <ref name="ref1" />).'']]
+[[File: nshb1.GIF |center|" Reaction of rice nsHb1 and SynHb with nitrite. The spectral changes associated with Rice nsHb1 <ref name="ref1" />).'']]
@@ Line 27: / Line 27: @@
 Class 1 rice nonsymbiotic hemoglobin (rice nsHb1) catalyze the reduction of hydroxylamine to ammonium at rates 100−2500 times faster than animal hemoglobins including myoglobin, neuroglobin, cytoglobin, and blood cell hemoglobin. These results support the hypothesis that plant contribute to anaerobic nitrogen metabolism in support of anaerobic respiration and survival during hypoxia.<ref name="ref3"/>
-[[File:Reaction_HA.GIF |right|thumb|150px|"Reaction of deoxyferrous Hbs with HA(from reference <ref name='ref3' />)"]]
+[[File:Reaction_HA.GIF |right|"Reaction of deoxyferrous Hbs with HA(from reference <ref name='ref3' />)"]]
-[[File:Hydroxylamine_reduction.GIF |center|thumb|"Relative rates of hydroxylamine reduction by different Hbs(from reference <ref name='ref3'/>)"]]
+[[File:Hydroxylamine_reduction.GIF |center|"Relative rates of hydroxylamine reduction by different Hbs(from reference <ref name='ref3'/>)"]]
 ===Expression===

@@ Line 2: / Line 2: @@
 ==Annotated Information==
 ===Function===
 May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule. Has an unusually high affinity for O2 because of a very low dissociation constant.
-、Rice nsHb1 have hypothetical roles in nitrogen metabolism
+====Rice nsHb1 have hypothetical roles in nitrogen metabolism====
 The reactions of class 1 rice nonsymbiotic Hb (rice nsHb1) with nitrate and nitrite suggested that these Hbs are not oxygen transporters and have hypothetical roles in nitrogen metabolism. And the deoxyferrous forms of each react rapidly with nitrite to form ferric Hb and ferrous-nitrosyl Hb in a fixed ratio, indicative of the production of nitric oxide from the reduction of nitrite by ferrous Hb.<ref name="ref1"/>
@@ Line 13: / Line 17: @@
-、Rice nsHb1 could serve as anaerobic nitrite reductases in vivo
+====Rice nsHb1 could serve as anaerobic nitrite reductases in vivo====
 Rate constants for nitrite reduction by a ferrous plant hemoglobin (rice nonsymbiotic hemoglobin 1) are more than 10 times faster than those observed for animal hemoglobins. These rate constants, along with the relatively high concentrations of nitrite present during hypoxia, suggest that plant hemoglobins could serve as anaerobic nitrite reductases in vivo .<ref name="ref2"/>
-[[File: nshb1_Reactivity.GIF |center|thumb||"Reactivity of nitrite and nitrate with other forms of rice nsHb1, SynHb, and Mb. (from reference <ref name="ref1" />)."]]
+[[File: nshb1_Reactivity.GIF |center|"Reactivity of nitrite and nitrate with other forms of rice nsHb1, SynHb, and Mb. (from reference <ref name="ref1" />)."]]
-、Rice nsHb1 catalyze the reduction of hydroxylamine to ammonium
+====Rice nsHb1 catalyze the reduction of hydroxylamine to ammonium====
 Class 1 rice nonsymbiotic hemoglobin (rice nsHb1) catalyze the reduction of hydroxylamine to ammonium at rates 100−2500 times faster than animal hemoglobins including myoglobin, neuroglobin, cytoglobin, and blood cell hemoglobin. These results support the hypothesis that plant contribute to anaerobic nitrogen metabolism in support of anaerobic respiration and survival during hypoxia.<ref name="ref3"/>

@@ Line 25: / Line 25: @@
 [[File:Reaction_HA.GIF |right|thumb|150px|"Reaction of deoxyferrous Hbs with HA(from reference <ref name='ref2' />)"]]
-[[File:Hydroxylamine_reduction.GIF |right|thumb|150px|"Relative rates of hydroxylamine reduction by different Hbs(from reference <ref name='ref2'/>)"]]
+[[File:Hydroxylamine_reduction.GIF |center|thumb|"Relative rates of hydroxylamine reduction by different Hbs(from reference <ref name='ref2'/>)"]]
 ===Expression===

@@ Line 9: / Line 9: @@
 The reactions of class 1 rice nonsymbiotic Hb (rice nsHb1) with nitrate and nitrite suggested that these Hbs are not oxygen transporters and have hypothetical roles in nitrogen metabolism. And the deoxyferrous forms of each react rapidly with nitrite to form ferric Hb and ferrous-nitrosyl Hb in a fixed ratio, indicative of the production of nitric oxide from the reduction of nitrite by ferrous Hb.<ref name="ref1"/>
-[[File:nshb1.gif]]
@@ Line 15: / Line 16: @@
 Rate constants for nitrite reduction by a ferrous plant hemoglobin (rice nonsymbiotic hemoglobin 1) are more than 10 times faster than those observed for animal hemoglobins. These rate constants, along with the relatively high concentrations of nitrite present during hypoxia, suggest that plant hemoglobins could serve as anaerobic nitrite reductases in vivo .<ref name="ref2"/>
-[[File:nshb1_Reactivity.gif]]
 、Rice nsHb1 catalyze the reduction of hydroxylamine to ammonium