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Scott, N. L., Xu, Y., Shen, G., Vuletich, D. A., Falzone, C. J., Li, Z., et al. (2010). Functional
and structural characterization of the 2/2 hemoglobin from
Synechococcus
sp. PCC 7002.
Biochemistry
,
49
, 7000-7011.
Shelnutt, J. A., Song, X. Z., Ma, J. G., Jia, S. L., Jentzen, W., & Medforth, C. J. (1998).
Nonplanar porphyrins and their significance in proteins.
Chemical Society Reviews
,
27
,
31-41.
Shibata, T., Matsumoto, D., Nishimura, R., Tai, H., Matsuoka, A., Nagao, S., et al. (2012).
Relationship between oxygen affinity and autoxidation of myoglobin.
Inorganic Chemis-
try
,
51
, 11955-11960.
Shikama, K. (2006). Nature of the FeO
2
bonding in myoglobin and hemoglobin: A new
molecular paradigm.
Progress in Biophysics and Molecular Biology
,
91
, 83-162.
Shikama, K., & Matsuoka, A. (2004). Structure-function relationships in unusual non-
vertebrate globins.
Critical Reviews in Biochemistry and Molecular Biology
,
39
, 217-259.
Smagghe, B. J., Sarath, G., Ross, E., Hilbert, J. L., & Hargrove, M. S. (2006). Slow ligand
binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal dif-
ferences between plants and other species.
Biochemistry
,
45
, 561-570.
Smagghe, B. J., Trent, J. T., III., & Hargrove, M. S. (2008). NO dioxygenase activity in
hemoglobins is ubiquitous in vitro, but limited by reduction in vivo.
PLoS One
,
3
, e2039.
Soule, T., Gao, Q. J., Stout, V., & Garcia-Pichel, F. (2013). The global response of
Nostoc
punctiforme
ATCC 29133 to UVA stress, assessed in a Temporal DNA microarray study.
Photochemistry and Photobiology
,
89
, 415-423.
Spiro, T. G., & Soldatova, A. V. (2012). Ambidentate H-bonding of NO and O
2
in heme
proteins.
Journal of Inorganic Biochemistry
,
115
, 204-210.
Springer, B. A., Sligar, S. G., Olson, J. S., & Philips, G. N., Jr. (1994). Mechanisms of ligand
recognition in myoglobin.
Chemical Reviews
,
94
, 699-714.
Stewart, J. J., & Coyne, K. J. (2011). Analysis of raphidophyte assimilatory nitrate reductase
reveals unique domain architecture incorporating a 2/2 hemoglobin.
Plant Molecular
Biology
,
77
, 565-575.
Sturms, R., DiSpirito, A. A., Fulton, D. B., & Hargrove, M. S. (2011). Hydroxylamine
reduction to ammonium by plant and cyanobacterial hemoglobins.
Biochemistry
,
50
,
10829-10835.
Sturms, R., DiSpirito, A. A., & Hargrove, M. S. (2011). Plant and cyanobacterial hemoglo-
bins reduce nitrite to nitric oxide under anoxic conditions.
Biochemistry
,
50
, 3873-3878.
Sugawara, Y., Kadono, E., Suzuki, A., Yukuta, Y., Shibasaki, Y., Nishimura, N., et al.
(2003). Hemichrome formation observed in human haemoglobin A under various buffer
conditions.
Acta Physiologica Scandinavica
,
179
, 49-59.
Tardif, M., Atteia, A., Specht, M., Cogne, G., Rolland, N., Brugiere, S., et al. (2012). Pre-
dAlgo: A new subcellular localization prediction tool dedicated to green algae.
Molecular
Biology and Evolution
,
29
, 3625-3639.
Teh, A.-H., Saito, J. A., Baharuddin, A., Tuckerman, J. R., Newhouse, J. S., Kanbe, M.,
et al. (2011). Hell's Gate globin I: An acid and thermostable bacterial hemoglobin resem-
bling mammalian neuroglobin.
FEBS Letters
,
585
, 3250-3258.
Thorsteinsson, M. V., Bevan, D. R., Ebel, R. E., Weber, R. E., & Potts, M. (1996). Spec-
troscopical and functional characterization of the hemoglobin of
Nostoc commune
UTEX
584 (Cyanobacteria).
Biochimica et Biophysica Acta
,
1292
, 133-139.
Thorsteinsson, M. V., Bevan, D. R., Potts, M., Dou, Y., Eich, R. F., Hargrove, M. S., et al.
(1999). A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability
properties.
Biochemistry
,
38
, 2117-2126.
Tiso, M., Tejero, J., Kenney, C., Frizzell, S., & Gladwin, M. T. (2012). Nitrite reductase
activity of nonsymbiotic hemoglobins
from
Arabidopsis
thaliana
.
Biochemistry
,
51
,
5285-5292.
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