Update on Biochemistry

Hbs are widely distributed in higher plants, and by comparing sequences, expression patterns, and ligand-binding properties, it is evident that these fall into two broad groups (Fig. 1; also see Andersson et al., 1996). The symbiotic-type Hbs are predominantly found in the infected cells of nitrogen-fixing nodules of legumes and nonlegumes and function to facilitate oxygen transport. The other group of plant Hbs, nonsymbiotic Hbs, appear to be ancestral to the symbiotic Hbs, are more widespread in the plant kingdom, and generally display a high affinity for oxygen. Their function in plants is the subject of much current inquiry (Appleby, 1992; Andersson et al., 1996; Arredondo-Peter et al., 1997a; Trevaskis et al., 1997; Hill, 1998). Some aspects of plant nonsymbiotic Hb function, particularly that of barley, have been succinctly reviewed by Hill (1998).

[1]  R. Hill,et al.  Haemoglobin expression in germinating barley , 1998, Seed Science Research.

[2]  R. Hill,et al.  Altering hemoglobin levels changes energy status in maize cells under hypoxia. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[3]  R. Hill,et al.  What are hemoglobins doing in plants , 1998 .

[4]  J. Olson,et al.  Rice Hemoglobins (Gene Cloning, Analysis, and O2-Binding Kinetics of a Recombinant Protein Synthesized in Escherichia coli) , 1997, Plant physiology.

[5]  D. Llewellyn,et al.  Two hemoglobin genes in Arabidopsis thaliana: the evolutionary origins of leghemoglobins. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[6]  R. Poole,et al.  Bacterial flavohaemoglobins: a consensus sequence and identification of a discrete enterobacterial group and of further bacterial globins. , 1997, FEMS microbiology letters.

[7]  M. B. Berry,et al.  Characterization of recombinant soybean leghemoglobin a and apolar distal histidine mutants. , 1997, Journal of molecular biology.

[8]  J. Bailey,et al.  Transgenic tobacco expressing Vitreoscilla hemoglobin exhibits enhanced growth and altered metabolite production , 1997, Nature Biotechnology.

[9]  M. Bolognesi,et al.  Nonvertebrate hemoglobins: structural bases for reactivity. , 1997, Progress in biophysics and molecular biology.

[10]  D. Llewellyn,et al.  A new hemoglobin gene from soybean: a role for hemoglobin in all plants. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[11]  J. Bailey,et al.  Effect of Vitreoscilla hemoglobin dosage on microaerobic Escherichia coli carbon and energy metabolism , 1996, Biotechnology and bioengineering.

[12]  G G Dodson,et al.  The structure of deoxy- and oxy-leghaemoglobin from lupin. , 1995, Journal of molecular biology.

[13]  W. Peacock,et al.  Symbiotic and nonsymbiotic hemoglobin genes of Casuarina glauca. , 1995, The Plant cell.

[14]  J. Tjepkema,et al.  Occurrence of hemoglobin in the nitrogen‐fixing root nodules of Alnus glutinosa , 1995 .

[15]  D. Goldberg The enigmatic oxygen-avid hemoglobin of Ascaris. , 1995, BioEssays : news and reviews in molecular, cellular and developmental biology.

[16]  I. Messana,et al.  The multiple functions of hemoglobin. , 1995, Critical reviews in biochemistry and molecular biology.

[17]  K. Dikshit,et al.  Oxygen dependent regulation of Vitreoscilla globin gene: evidence for positive regulation by FNR. , 1994, Biochemical and biophysical research communications.

[18]  G. Sarath,et al.  Characteristics of Modified Leghemoglobins Isolated from Soybean (Glycine max Merr.) Root Nodules , 1994, Plant physiology.

[19]  G. Sarath,et al.  Cloning and Sequence Analysis of a cDNA Encoding Ferric Leghemoglobin Reductase from Soybean Nodules , 1994, Plant physiology.

[20]  O. H. Kapp,et al.  Adventitious variability? The amino acid sequences of nonvertebrate globins. , 1993, Comparative biochemistry and physiology. B, Comparative biochemistry.

[21]  H. Zhu,et al.  Yeast flavohemoglobin is an ancient protein related to globins and a reductase family. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[22]  D. Webster,et al.  The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases. , 1992, Archives of biochemistry and biophysics.

[23]  W. Jakob,et al.  NADH-dependent methemoglobin reductase from the obligate aerobe Vitreoscilla: improved method of purification and reexamination of prosthetic groups. , 1992, Archives of biochemistry and biophysics.

[24]  T. Wang,et al.  Kinetics and thermodynamics of oxygen, CO, and azide binding by the subcomponents of soybean leghemoglobin. , 1990, The Journal of biological chemistry.

[25]  D. Llewellyn,et al.  Nonlegume hemoglobin genes retain organ-specific expression in heterologous transgenic plants. , 1990, The Plant cell.

[26]  Q. Gibson,et al.  The kinetics of ligand binding to plant hemoglobins. Structural implications. , 1989, The Journal of biological chemistry.

[27]  W. Peacock,et al.  A role for haemoglobin in all plant roots , 1988 .

[28]  W. Peacock,et al.  Common evolutionary origin of legume and non-legume plant haemoglobins , 1986, Nature.