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Volume 272, Number 5, Issue of January 31, 1997 pp. 3000-3006
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Solution of ¹H NMR Structure of the Heme Cavity in the Oxygen-avid Myoglobin from the Trematode Paramphistomum epiclitum

(Received for publication, July 3, 1996, and in revised form, October 28, 1996)

Wei Zhang , Khwaja A. Rashid ^§ , Masoodul Haque ^¶ , Ather H. Siddiqi ^¶ , Serge N. Vinogradov , Luc Moens ^§ and Gerd N. La Mar

From the  Department of Chemistry, University of California, Davis, California 95616, the ^§ Department of Biochemistry, University of Antwerp (UIA), B-2610 Antwerp, Belgium, the ^¶ Department of Zoology, A.M. University, Aligarh, India 202002, and the  Department of Biochemistry, School of Medicine, Wayne State University, Detroit, Michigan 48201

A two-dimensional ¹H NMR study has been carried out on the heme cavity of the extreme oxygen-avid and autoxidation-resistant oxy-myoglobin complex from the trematode Paramphistomum epiclitum, and the residues were identified which potentially provide hydrogen bond stabilization for the bound oxygen. Complete assignment of the heme core resonances allows the identification of 10 key heme pocket residues, 4 Phe, 4 Tyr, and 2 upfield ring current aliphatic side chains. Based solely on the conserved myoglobin folding topology that places the E helix-heme crossover and the completely conserved Phe(CD1)-heme contact at opposing meso positions, the heme orientation in the cavity and the E helix alignment were unambiguously established that place Tyr⁶⁶ at position E7. Moreover, all eight aromatic and the two aliphatic side chains were shown to occupy the positions in the heme cavity predicted by amino acid sequence alignment with globins of known tertiary structure. The dipolar contacts for the Tyr³²(B10) and Tyr⁶⁶(E7) rings indicate that both residues are oriented into the heme cavity, which is unprecedented in globins. The ring hydroxyl protons for both Tyr are close to each other and in a position to provide hydrogen bonds to the coordinated oxygen, as supported by strong retardation of their exchange rate with bulk solvent. A more crowded and compact structure increases the dynamic stability of the distal pocket and may contribute to the autoxidation resistance of this myoglobin.

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