@article {2424,
	title = {Calcium-dependent conformation of a heme and fingerprint peptide of the diheme cytochrome c peroxidase from Paracoccus pantotrophus},
	journal = {Biochemistry},
	volume = {40},
	number = {22},
	year = {2001},
	note = {<p>Times Cited: 8</p>
},
	month = {Jun 5},
	pages = {6570-6579},
	abstract = {<p>The structural changes in the heme macrocycle and substituents caused by binding of Ca2+ to the diheme cytochrome c peroxidase from Paracoccus pantotrophus were clarified by resonance Raman spectroscopy of the inactive fully oxidized form of the enzyme. The changes in the macrocycle vibrational modes are consistent with a Ca2+-dependent increase in the out-of-plane distortion of the low-potential heme, the proposed peroxidatic heme. Most of the increase in out-of-plane distortion occurs when the high-affinity site I is occupied, but a small further increase in distortion occurs when site II is also occupied by Ca2+ or Mg2+. This increase in the heme distortion explains the red shift in the Soret absorption band that occurs upon Ca2+ binding. Changes also occur in the low-frequency substituent modes of the heme, indicating that a structural change in the covalently attached fingerprint pentapeptide of the LP heme occurs upon Ca2+ binding to site I. These structural changes may lead to loss of the sixth ligand at the peroxidatic heme in the semireduced form of the enzyme and activation.</p>
},
	isbn = {0006-2960},
	url = {http://dx.doi.org/10.1021/bi002870z},
	author = {Pauleta, S. R. and Lu, Y. and Goodhew, C. F. and Moura, I. and Pettigrew, G. W. and Shelnutt, J. A.}
}
