To isolate a new P450 monooxygenase belonging to the CYP102 family, CYP102H1 of Nocardia farcinica IFM 10152 (i.e., pnf11580) was cloned, expressed, and partially characterized. CYP102H1 gene was amplified from pNF1 of N. farcinica and cloned into expression vectors (i.e., pTrc99A, pET28a(+)). When Escherichia coli BL21(DE3) codon+ strain was transformed with pET28a-CYP102H1 and the culture was induced with 1.0 mM isopropyl-${eta}$-D-thio-galactoside in a complex medium at $30^{circ}C$, CYP102H1 could be expressed in soluble form even though soluble form was not dominant. The enzyme showed typical features of heme proteins; a spectrum of reduced CO bound form showed typical maximum at 450 nm. When the biotransformation of linoleic acid was carried out in a reconstituted system consisting of CYP102H1 and redox partner proteins of Pseudomonas putida (i.e., CamAB), ${omega}1$-hydroxylinoleic acid was detected with gas chromatography/mass spectrometry analysis, suggesting that CYP102H1 catalyzes oxygenation of linoleic acid at ${omega}$-1 position, which is typical in CYP102A subfamily members.